研究成果

 

2018年の研究業績

今高 寛晃（兵庫県立大学・大学院工学研究科　教授）

1. Machida K, Kanzawa K, Shigeta T, Yamamoto Y, Tsumoto K, and *Imataka H
Huntingtin polyglutamine-dependent protein aggregation in reconstituted cells.
ACS synthetic Biology 7: 377-383 (2018) doi: 10.1021/acssynbio.7b00372
2. Uemura E, Niwa T, Minami S, Takemoto K, Fukuchi S, Machida K, Imataka H, Ueda T, Ota M, and Taguchi H
Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.
Scientific Reports 8: 678 (2018) doi: 10.1038/s41598-017-18977-5
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岩川 弘宙（東京大学・定量生命科学研究所・助教）

1. Baeg K, Tomari Y, *Iwakawa HO
In vitro RNA-dependent RNA Polymerase Assay Using Arabidopsis RDR6
Bio-protocol 8(1), (2018)
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田中 元雅（独立行政法人理化学研究所 脳科学総合研究センター　チームリーダー）

1. Chen, C. W. and Tanaka, M.
Genome-wide Translation Profiling by Ribosome-Bound tRNA　Capture.
Cell Rep. 23, 608-621, (2018). doi: 10.1016/j.celrep.2018.03.035.
プレスリリース： http://www.riken.jp/pr/press/2018/20180411_1/
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門倉　広（東北大学・多元物質科学研究所　准教授）

1. Yuichi Tsuchiya, Michiko Saito, Hiroshi Kadokura, Jun-ichi Miyazaki, Fumi Tashiro, Yusuke Imagawa, Takao Iwawaki, Kenji Kohno
IRE1–XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells
J. Cell Biol. 217 (2018) DOI: 10.1083/jcb.201707143
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河野　憲二（奈良先端科学技術大学院大学・バイオサイエンス研究科　教授）

1. Tsuchiya, Y., Saito, M., Kadokura, H., Miyazaki, J., Tashiro, F., Imagawa, Y., Iwawaki, T., and Kohno, K.*
IRE1-XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells.
J. Cell Biol. 217(4), 1287-1301 (2018) doi: 10.1083/jcb.201707143.
プレスリリース：http://www.naist.jp/pressrelease/2018/03/004316.html
2. Mai, C.T., Le, Q.G., Ishiwata-Kimata, Y., Takagi, H., Kohno, K., and Kimata. Y.* 4-Phenylbutyrate suppresses the unfolded protein response without restoring protein folding in Saccharomyces cerevisiae.
FEMS Yeast Research, 18(2), (2018) doi: 10.1093/femsyr/foy016.
3. Yamaoka, Y., Choi, B.Y., Kim, H., Shin, S., Kim, Y., Jang, S., Song, W.Y., Cho, C.H., Yoon, H.S., Kohno, K., and Lee, Y.*
Identification and functional study of ER stress sensor IRE1 in Chlamydomonas reinhardtii.
Plant J., 94(1), 91-104 (2018) doi: 10.1111/tpj.13844.
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藤木　幸夫（九州大学生体防御医学研究所　特任教授）

1. Okumoto, K., Ono, T., Toyama, R., Shimomura, A., Nagata, A., and Fujiki Y.
New splicing variants of mitochondrial Rho GTPase-1 (Miro1) transport peroxisomes.
J. Cell Biol., 217, 619-633 (2018). doi: 10.1083/jcb.201708122.
紹介記事(日本語)
日本語記事（PDF)
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千葉 志信（計画研究代表者 京都産業大学・准教授）

1. Fujiwara, K., Ito, K., Chiba, S..
MifM-instructed translation arrest involves nascent chain interactions with the exterior as well as the interior of the ribosome.
Sci Rep. 8, 10311. (2018) doi: 10.1038/s41598-018-28628-y.
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姚 閔（北海道大学大学院　先端生命科学研究院　X線構造生物学研究室）

1. Takehito Tanzawa, Koji Kato, Dylan Girodat, Toyoyuki Ose, Yuki Kumakura, Hans-Joachim Wieden, Toshio Uchiumi, Isao Tanaka, and Min Yao The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.
Nucleic Acids Research. 46, 3232-3244 (2018)
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齋尾 智英（北海道大学　大学院理学研究院　化学部門　構造化学研究室）

1. Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the Trigger Factor chaperone
S Kawagoe, H Nakagawa, H Kumeta, K Ishimori, T Saio
Journal of Biological Chemistry, in press
http://www.jbc.org/content/early/2018/08/09/jbc.RA118.003579
2. Saio T, Kawagoe S, Ishimori K, Kalodimos CG.
Oligomerization of a molecular chaperone modulates its activity.
Elife. 2018 May 1;7. pii: e35731. doi: 10.7554/eLife.35731.
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池内 与志穂（東京大学　生産技術研究所　准教授 ）

1. Umegaki Y, Brotons AM, Nakanishi Y, Luo Z, Zhang H, Bonni A, Ikeuchi Y.
Palladin Is a Neuron-Specific Translational Target of mTOR Signaling That Regulates Axon Morphogenesis.
Journal of Neuroscience. 2018 May 23;38(21):4985-4995. doi: 10.1523/JNEUROSCI.2370-17.2018.
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森　博幸（京都大学　ウイルス・再生医科学研究所）

1.

  1. Mori, H.*, Sakashita, S., Ito, J., Ishii, E. and Akiyama, Y.
    Identification and characterization of arrest motif in VemP by systematic mutational analysis.
    J. Biol. Chem. 293, 2915-2926 (2018) doi:10.1074/jbc.M117.816561
2.

  1. Miyazaki, R., Myogo, N., Mori, H. and Akiyama, Y.*
    A new photo-cross-linking approach for analysis of protein dynamics in vivo.
    J. Biol. Chem. 293, 677-686 (2018). doi:10.1074/jbc.M117.817270
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西頭 英起（宮崎大学・医学部機能生化学 教授）

1.

Kadowaki, H., Satrimafitrah, P., Takami, Y. and Nishitoh H.
Molecular mechanism of ER stress-induced pre-emptive quality control involving association of the translocon, Derlin-1, and HRD1.
Sci. Rep. 8, 7317. (2018). doi:10.1038/s41598-018-25724-x.
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阪口 雅郎（兵庫県立大学・大学院生命理学研究科）

1.

Kida, Y. and Sakaguchi, M.
Interaction mapping of the Sec61 translocon identifies two Sec61α regions interacting with hydrophobic segments in translocating chains.
J. Biol. Chem. 293, 17050-17060 (2018) doi: 10.1074/jbc.RA118.003219
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岩崎 信太郎（国立研究開発法人　理化学研究所　主任研究員）

1.
  1. Iwasaki S, Iwasaki W, Takahashi M, Sakamoto A, Watanabe C, Shichino Y, Stephen N. Floor, Fujiwara K, Mito M, Dodo K, Sodeoka M, Imataka H, Honma T, Fukuzawa K, Ito T, Nicholas T. Ingolia.
    The Translation Inhibitor Rocaglamide Targets a Bimolecular Cavity between eIF4A and Polypurine RNA.
    Molecular Cell　(2018) in press.
2.
  1. Akichika S, Hirano S, Shichino Y, Suzuki T, Nishimasu H, Ishitani R, Sugita A, Hirose Y, Iwasaki S, Nureki O, Suzuki T.
    Cap-specific terminal N6-methylation of RNA by an RNA polymerase II–associated methyltransferase.
    Science (2018) in press. DOI: 10.1126/science.aav0080
3.
  1. Taiwa K, Yokoi S, Mito M, Fujii K, Kimura Y, Iwasaki S, Nakagawa S.
    UPA-Seq:Prediction of Functional LncRNAs Using Differential Sensitivity to UV Crosslinking.
    RNA. 2018 in press
4.
  1. Kurihara Y, Makita Y, Kawashima M, Fujita T, Iwasaki S, Matsui M.
    Transcripts from downstream alternative transcription start sites evade uORF-mediated inhibition of gene expression in Arabidopsis.
    Proc Natl Acad Sci U S A. (2018) in press. doi: 10.1073/pnas.1804971115.
5.
  1. Naruse K, Matsuura-Suzuki E, Watanabe M, Iwasaki S, Tomari Y.
    In vitro reconstitution of chaperone-mediated human RISC assembly.
    RNA. 24, 6-11, (2018). doi: 10.1261/rna.063891.117.
6.
  1. Iwasaki S, Tomari Y.
    Reconstitution of RNA Interference Machinery.
    Methods Mol Biol. 1680, 131-143, (2018). doi: 10.1007/978-1-4939-7339-2_9.
7.
  1. Mito M, Kadota M, Tanaka K, Furuta Y, Abe K, Iwasaki S, Nakagawa S.
    Cell Type-Specific Survey of Epigenetic Modifications by Tandem Chromatin Immunoprecipitation Sequencing.
    Sci Rep. 8, 1143 (2018). doi: 10.1038/s41598-018-19494-9.

press release
http://www.riken.jp/pr/press/2018/20180130_2/
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佐伯 泰（公益財団法人東京都医学総合研究所 蛋白質代謝研究室 副参事研究員）

1.

Tsuchiya, H., Burana, D., Ohtake, F., Arai, N., Kaiho, A., Komada, M., Tanaka, K., and Saeki, Y.
Ub-ProT reveals global length and composition of protein ubiquitylation in cells.
Nature Commun. 9, 524 (2018) doi: 10.1038/s41467-018-02869-x
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2017年の研究業績

田口 英樹（領域代表・東京工業大学・教授）

1. Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T.,Chiba, S., Ito, K. and Taguchi, H.
Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.
Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020.
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今高 寛晃（兵庫県立大学・大学院工学研究科　教授）

1. Daiko Y, Mizutani S, Machida K. Imataka H, Honda S and Iwamoto Y
H+ emission under room temperature and non-vacuumatmosphere from a sol–gel-derived nanoporous emitter
J Sol-Gel Sci. Technol. 83: 252-258 (2017) doi:10.1007/s10971-017-4430-z
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稲田 利文（東北大学・大学院薬学研究科　教授）

1.
  1. Matsuo, Y., Ikeuchi, K., Saeki, Y., Iwasaki, S., Schmidt, C., Udagawa, T., Sato, F., Tsuchiya, H., Becker, T., Tanaka, K., Ingolia, NT., Beckmann, R. and *Inada, T.
    Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control.
    Nat. Commun. DOI 10.1038/s41467-017-00188-1 (2017)
2.

  1. Sugiyama T, Nobuta R, Ando K, Matsuki Y,  *Inada, T.
    Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product. Biochem Biophys Res Commun. 488, 122-128. doi: 10.1016/j.bbrc.2017.05.0 (2017)
3.

*Inada, T.
【Review】The ribosome as a platform for mRNA and nascent polypeptide quality control.

Trends Biochem. Sci. 42, 5-15 (2017)
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長尾 翌手可（研究分担者 東京大学・助教）

1. Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T.,Chiba, S., Ito, K. and Taguchi, H.
Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.
Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020.
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岩川 弘宙（東京大学・定量生命科学研究所・助教）

1. *Iwakawa HO, *Tomari Y
Silencing messages in a unique way
Nature Plants 3(10), 769-770.(2017)
2. Watanabe M, Iwakawa HO, Tadakuma H, Tomari Y
Biochemical and single-molecule analyses of the RNA silencing suppressing activity of CrPV-1A
Nucleic acids research 45(18), 10873-10844.(2017)
3. Tajima Y, Iwakawa HO, Hyodo K, Kaido M, Mise K, Okuno T
Requirement for eukaryotic translation initiation factors in cap-independent translation differs between bipartite genomic RNAs of red clover necrotic mosaic virus
Virology 509,152-158. (2017)
4.

Tomari Y, *Iwakawa HO
In Vitro Analysis of ARGONAUTE-Mediated Target Cleavage and Translational Repression in Plants
Methods in Molecular Biology 1640, 55-71. (2017)
5.
  1. Kyungmin Baeg, Hiro-oki Iwakawa*, Yukihide Tomari* (*corresponding authors)
    The poly(A) tail blocks RDR6 from converting self mRNAs into substrates for gene silencing
    Nature Plants, 20 March 2017 | Volume: 3 | Article number: 17036, doi:10.1038/nplants.2017.36
    またこの論文はNature Plants ４月号の表紙を飾りました。
    広報記事
    1. プレスリリース
    http://www.iam.u-tokyo.ac.jp/pressrelease/170321/
    2. EurekAlert!
    https://www.eurekalert.org/pub_releases/2017-03/uot-hpc031717.php
    3. UTokyo research
    http://www.u-tokyo.ac.jp/ja/utokyo-research/research-news/how-plants-can-tell-friend-from-foe.html
    報道
    日経産業新聞 2017年4月7日 8ベージ
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稲葉 謙次（東北大学・多元物質科学研究所　教授）

1.
  1. Maegawa, K., Watanabe, S., Noi, K., Okumura, M., Amagai, Y., Inoue, M., Ushioda, R., Nagata, K., Ogura, T. and Inaba, K.*
    The highly dynamic nature of ERdj5 is key to efficient elimination of aberrant protein oligomers through ER-associated degradation
    Structure, 6, 646-857(2017)
    URL: http://www.cell.com/structure/fulltext/S0969-2126(17)30102-8
    雑誌の表紙を飾りました！ http://www.cell.com/structure/issue?pii=S0969-2126(16)X0007-X

    プレスリリース http://www2.tagen.tohoku.ac.jp/lab/news_press/20170508/

    報道： 日経新聞　電子版（2017/05/05）
    日経バイオテク ONLINE（2017/05/09）
    J-Net21 中小企業ビジネス支援サイト（2017/05/09）
    医療NEWS QLifePro（2017/05/10）
    日刊工業新聞：https://www.nikkan.co.jp/articles/view/00429701（2017/05/26）
2.
  1. Arai, K., Takei, T., Okumura, M., Watanabe, S., Amagai, Y., Asahina, Y., Moroder, L., Hojo, H.*, Inaba, K.* and Iwaoka, M.* (*co-corresponding authors)
    Preparation of selenoinsulin as a long-lasting insulin analog
    Angewandte Chemie 56, 5522-5526 (2017)
    URL: http://onlinelibrary.wiley.com/doi/10.1002/anie.201701654/abstract;jsessionid=9D67E954D8C07ACCE4F16024679DCDCD.f03t04

    プレスリリース http://www2.tagen.tohoku.ac.jp/lab/news_press/20170411/

    報道： 日経新聞　電子版（2017/05/05）
    日経バイオテク ONLINE（2017/05/09）
    医療NEWS QLifePro（2017/05/10）
    日刊工業新聞（2017/04/14）* 閲覧には会員登録（無料）が必要です
    m3.com（2017/04/14）* 閲覧には会員登録（無料）が必要です
    マイナビニュース（2017/04/14）
    糖尿病ネットワーク（2017/04/14）
    大学ジャーナルONLINE（2017/04/16）
3.

  1. Watanabe, S., Harayama, M., Kanemura, S., Sitia, R. and Inaba, K.*
    Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface
    Proc Natl Acad Sci U S A. 114, 3224-3232 (2017)
    URL: http://www.pnas.org/content/114/16/E3224.long
    プレスリリース：http://www2.tagen.tohoku.ac.jp/lab/news_press/20170404/
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河野　憲二（奈良先端科学技術大学院大学・バイオサイエンス研究科　教授）

1. Tschurtschenthaler, M., Adolph, T.E., Ashcroft, J.W., Niederreiter, L., Bharti, R., Saveljeva, S., Bhattacharyya, J., Flak, M.B., Shih, D.Q., Fuhler, G.M., Parkes, M., Kohno, K., Iwawaki, T., van der Woude, C.J., Harding, H., Smith, A.M. Peppelenbosch, M.P., Targan, S.R., Ron, D., Rosenstiel, P., Blumberg, R.S.*, and Kaser, A.*
Defective ATG16L1-mediated removal of IRE1α drives Crohn's disease-like ileitis.
J. Exp. Med. 214(2), 401-422 (2017) doi: 10.1084/jem.20160791
2. Sato, H., Shiba, Y.*, Tsuchiya, Y., Saito, M., and Kohno, K.* 4μ8C inhibits insulin secretion independent of IRE1α RNase activity.
Cell Struct. Funct. 42(1), 61-70 (2017) doi: 10.1247/csf.17002. Epub 2017 Mar 18. PMID: 28321016
3. Schmitner, N., Kohno, K. and Meyer, D*. Ptf1a+, ela3l- cells are developmentally maintained progenitors for exocrine regeneration following extreme loss of acinar cells in zebrafish larvae.
Dis. Model. Mech. 10(3), 307-321 (2017) doi: 10.1242/dmm.026633
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藤木　幸夫（九州大学生体防御医学研究所　特任教授）

1. Kinoshita, N., Matsuura, A., and Fujiki Y.
Peroxisome biogenesis: a novel inducible PEX19 splicing variant is involved in early stages of peroxisome proliferation.
J. Biochem. 161, 297-308 (2017).
2. Yagita, Y., Shinohara, K., Liu, Y., and Fujiki Y.
ACBD5 is a peroxisomal tail-anchored protein exposing its acyl-CoA binding domain to the cytosol.
J. Biol. Chem. 292, 691-705 (2017).
3. Imoto, Y., Abe, Y., Okumoto, K., Honsho, M., Kuroiwa, H., Kuroiwa, T., and Fujiki Y.
Defining dynamin-based ring organizing center on the peroxisome-dividing machinery isolated from Cyanidioschyzon merolae..
J. Cell Sci. 130, 853-867 (2017) (Highlighted articleとして掲載)
4. Abe, S., Nagai, T., Masukawa, M., Okumoto, K., Homma, Y., Fujiki Y., and Mizuno, K.
Localization of NDR2 to peroxisomes and its role in ciliogenesis.
J. Biol. Chem. 292, 4089-4098 (2017).
5. Honsho, M., Abe, Y., and Fujiki Y.
Plasmalogen synthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet
of plasma membrane.
Sci. Rep. 7, article 43936 (2017).
6. Okumoto, K., Tamura, S., and Fujiki Y.
Blue-Native PAGE: Applications to study on peroxisome biogenesis.
Methods in Mol. Biol. 1595, 197-205 (2017)
7. Liu,Y., Honsho, M., and Fujiki Y.
In vitro PMP import analysis using cell-free synthesized PMP and isolated peroxisomes.
Methods in Mol. Biol. 1595, 207-212 (2017)
8. Okumoto, K., Honsho, M., Liu, Y., and Fujiki Y.
Peroxisomal membrane and matrix protein import using a semi-intact mammalian cell system.
Methods in Mol. Biol. 1595, 213-219 (2017)
9. Fujiki Y.
Functional complementation (version 3.0).
eLS., article A27640 (2017).
10.
  1. Hosoi KI, Miyata N, Mukai S, Furuki S, Okumoto K, Cheng EH, Fujiki Y.
    The VDAC2-BAK axis regulates peroxisomal membrane permeability.
    J Cell Biol. 2017. 216, 709-722. doi: 10.1083/jcb.201605002.
    紹介記事（日本語）
    日本語記事（PDF)
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千葉 志信（計画研究代表者 京都産業大学・准教授）

1. Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T., Chiba, S., Ito, K. and Taguchi, H.
Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.
Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020.
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姚 閔（北海道大学大学院　先端生命科学研究院　X線構造生物学研究室）

1. Meirong Chen, Koji Kato, Yume Kubo, Yoshikazu Tanaka, Yuchen Liu, Feng Long, William Whitman, Pascal Lill, Christos Gatsogiannis, Stefan Raunser,Nobutaka Shimizu, Akira Shinoda, Akiyoshi Nakamura, Isao Tanaka, and Min Yao.
Structural basis for the tRNA-dependent cysteine biosynthesis
Nature Communications. 8, 1512 (2017)
2. Minghao Chen, Shin-ichi Asai, Shun Narai, Shusuke Nambu, Naoki Omura, Yuriko Sakaguchi, Tsutomu Suzuki, Masao Ikeda-Saito, Kimitsuna Watanabe, Min Yao, Naoki Shigi, and Yoshikazu Tanaka.
Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA
Proc. Natl. Acad. Sci. USA, 114, 4954-4959 (2017)
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高橋 広夫（千葉大学・大学院園芸学研究科・応用生命化学領域 准教授

1. Vial-Pradel S., Keta S., Nomoto M., Luo L., Takahashi H., Suzuki M., Yokoyama Y., Sasabe M., Kojima S., Tada Y., *Machida Y.and *Machida C.
Arabidopsis zinc-finger-like protein ASYMMETRIC LEAVES2 (AS2) and two nucleolar proteins maintain gene body DNA methylation in the leaf polarity gene ETTIN (ARF3),
Plant Cell Physiol.(DOI: 10.1093/pcp/pcy031)
2. Hayashi N., Sasaki S., Takahashi H., Yamashita Y., Naito S., *Onouchi H. Identification of Arabidopsis thaliana upstream open reading frames encoding peptide sequences that cause ribosomal arrest.
Nucleic Acids Res., 45, 8844-8858, (2017) DOI: 10.1093/nar/gkx528
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池内 与志穂（東京大学　生産技術研究所　准教授）

1. Kawada J, Kaneda S, Kirihara T, Maroof A, Levi T, Eggan K, Fujii T, Ikeuchi Y.
Generation of a Motor Nerve Organoid with Human Stem Cell-Derived Neurons.
Stem Cell Reports. 2017 Nov 14;9(5):1441-1449. doi: 10.1016/j.stemcr.
2017.09.021.
報道：
朝日新聞（2017/10/27、朝刊）
化学工業日報（2017/10/27、朝刊）
日本経済新聞（2017/10/27、夕刊）
毎日新聞（2017/10/28、夕刊）
読売新聞（2017/11/1、夕刊）
科学新聞（2017/11/3、1面）
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森　博幸（京都大学　ウイルス・再生医科学研究所）

1.

  1. Daimon, Y., Masui, C., Tanaka, Y., Shiota, T., Suzuki, T., Miyazaki, R., Sakurada, H., Lithgow, T., Dohmae, N., Mori, H., Tsukazaki, T.*, Narita, S.* and Akiyama, Y*.
    BepA mediates productive transfer of substrate proteins to the b-barrel assembly machinery (BAM) complex.
    Mol. Microbiol. 106, 760-776 (2017) doi: 10.1111/mmi.13844
2.

  1. Furukawa, A., Yoshikaie, K., Mori, T., Mori, H., Morimoto, Y. V., Sugano, Y., Iwaki, S., Minamino, T., Sugita, Y., Tanaka, Y. and Tsukazaki, T.*
    Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF
    Cell Reports 19, 895-901. (2017)
3.
  1. 石井英治*、森　博幸

「ビブリオ属細菌における２つのタンパク質膜透過促進因子の生理的意義と使い分け機構」
医学の歩み, 261, 1178-1179 (2017)
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西頭 英起（宮崎大学・医学部機能生化学 教授）

1.

Murao, N. and Nishitoh H.
Role of the unfolded protein response in the development of central nervous system.
J. Biochem. 162,155-162. (2017). doi: 10.1093/jb/mvx047.
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岩崎 信太郎（国立研究開発法人　理化学研究所　主任研究員）

1.

  1. Matsuo, Y., Ikeuchi, K., Saeki, Y., Iwasaki S., Schmidt, C., Udagawa, T., Sato, F., Tsuchiya, H., Becker, T., Tanaka, K., Ingolia, NT., Beckmann, R. and *Inada, T.
    Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control.
    Nat. Commun. DOI 10.1038/s41467-017-00188-1 (2017)
2.

  1. Iwasaki S, Ingolia NT.
    The Growing Toolbox for Protein Synthesis Studies.
    Trends Biochem Sci. 8, 612-624 (2017). doi: 10.1016/j.tibs.2017.05.004. (2017)
3.
  1. 七野悠一、岩崎信太郎 
    リボソームプロファイリングが切り拓く翻訳研究の未来
    実験医学 Vol. 25, No. 11, （7月号）　2017　p1868-1873
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2016年の研究業績

田口 英樹（領域代表・東京工業大学・教授）

1.

Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito
Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing
Proc. Natl. Acad. Sci. USA 113 (2016)  doi:10.1073/pnas.1520560113
http://www.pnas.org/content/early/2016/01/27/1520560113.abstract

広報記事
タンパク質合成過程における「緩急のリズム」を実証 -大腸菌遺伝子産物中間状態を網羅的に解析-
http://www.kyoto-su.ac.jp/news/20160205_345_release_ka02.html
http://www.titech.ac.jp/news/2016/033388.html
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今高 寛晃（兵庫県立大学・大学院工学研究科　教授）

1. Machida K, Shigeta T, Kobayashi A, Masumoto A, Hidaka Y and *Imataka H
Cell-free analysis of polyQ-dependent protein aggregation and its inhibition by chaperone proteins
J. Biotechnology 239:1-8 (2016) doi: 10.1016/j.jbiotec.2016.09.031
2. Kashiwagi K, Shigeta T, Imataka H, Ito T, and Yokoyama S
Expression, purification, and crystallization of Schizosaccharomyces pombe eIF2B
J. Structural and Functional Genomics 17: 33-38 (2016) doi:10.1007/s10969-016-9203-3
3. Ozdemir A, Machida K, Imataka H, and Catling A
Identification of the T-complex protein as a binding partner for newly synthesized Cytoplasmic Dynein Intermediate
Biochem. Biophys. Res. Commun. 469: 126-131 (2016) doi: 10.1016/j.bbrc.2015.11.082
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稲田 利文（東北大学・大学院薬学研究科・教授）

1. Ikeuchi, K., Yazaki, E., Kudo, K. and *Inada, T.
Conserved functions of human Pelota in mRNA quality controls for nonstop mRNA.
FEBS Let. 18, 3254-3263 (2016)
2. Ikeuchi, K. and *Inada, T.
Ribosome-associated Asc1/RACK1 is required for endonucleolytic cleavage induced by stalled ribosome at the 3' end of nonstop mRNA.
Sci. Rep. 6, 28234. (2016)
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稲葉　謙次（東北大学・多元物質科学研究所　教授）

1.

Kanemura, S., Okumura, M., Yutani, K., Ramming, T., Hikima, T., Appenzeller-Herzog, C. , Akiyama, S. and Inaba, K.* "Human ER oxidoreductin-1a (Ero1a) undergoes dual regulation through complementary redox interactions with protein-disulfide isomerase", J. Biol. Chem., 291, 23952-23964 (2016)
URL: http://www.jbc.org/content/291/46/23952.long
2.

Ryo Ushioda, Akitoshi Miyamotod, Michio Inoue, Satoshi Watanabe, Masaki Okumurae, Ken-ichi Maegawa, Kaiku Uegaki, Shohei Fujii, Yasuko Fukuda, Masataka Umitsu, Junichi Takagi, Kenji Inaba, Katsuhiko Mikoshiba and Kazuhiro Nagata
Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5
Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6055-E6063. Epub 2016 Sep 30., doi: 10.1073/pnas.1605818113
http://www.pnas.org/content/113/41/E6055

プレスリリース
ジスルフィド還元酵素ERdj5がSERCA2bのジスルフィド結合を還元することを解明
http://www.kyoto-su.ac.jp/news/20161001_345_kenkyu_masu01.html

報道

産経新聞（2016年10月3日付23面)、京都新聞（2016年10月1日付33面）、共同通信（オンライン）、日経プレスリリース（オンライン）
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河野　憲二（奈良先端科学技術大学院大学・バイオサイエンス研究科　教授）

1. Kanda, S., Yanagitani, K.*, Yokota, Y., Esaki, Y., and Kohno, K.* Autonomous translational pausing is required for XBP1u mRNA recruitment to the ER via the SRP pathway.
Proc Natl Acad Sci USA, 113(40), E5885-E5895 (2016) doi: 10.1073/pnas.1604435113, PMID: 27651490
紹介記事
http://bsw3.naist.jp/research/index.php?id=1377
報道
朝日新聞(11月3日朝刊21面),　日刊工業新聞(9月21日朝刊27面)
2. Le, Q.G,, Ishiwata-Kimata, Y., Kohno, K. and Kimata, Y.* Cadmium impairs protein folding in the endoplasmic reticulum and induces the unfolded protein response.
FEMS Yeast Research 16(5), pii: fow049 (1-8) (2016) doi: 10.1093/femsyr/fow049
3. Tsuru, A., Imai, Y., Saito, M., and Kohno, K.
Novel mechanism of enhancing IRE1α-XBP1 signalling via the PERK-ATF4 pathway.
Sci. Rep. Apr 7; 6:24217 (2016) doi: 10.1038/srep24217, PMID:27052593
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藤木　幸夫（九州大学生体防御医学研究所　特任教授）

1. Honsho, M., Yamashita,S., and Fujiki Y.
Peroxisome homeostasis: mechanisms of division and selective degradation of peroxisomes in mammals.
Biochim. Biophys. Acta-Mol. Cell Res. 1863, 984-991 (2016).
2. Fujiki Y.
Peroxisome biogenesis and human peroxisome-deficiency disorders.
Proc. Jpn. Acad., Ser. B 92: 463-477 (2016).
3. Liu Y., Yagita Y., and Fujiki Y.
Assembly of peroxisomal membrane proteins via the direct Pex19p-Pex3p pathway.
Traffic 17, 433-455 (2016) doi: 10.1111/tra.12376
紹介文
liu-et_al.pdf
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千葉 志信（計画研究代表者 京都産業大学・准教授）

1.

Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito
Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing
Proc. Natl. Acad. Sci. USA 113 (2016)  doi:10.1073/pnas.1520560113
http://www.pnas.org/content/early/2016/01/27/1520560113.abstract

広報記事
タンパク質合成過程における「緩急のリズム」を実証 -大腸菌遺伝子産物中間状態を網羅的に解析-
http://www.kyoto-su.ac.jp/news/20160205_345_release_ka02.html
http://www.titech.ac.jp/news/2016/033388.html
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伊藤 維昭（研究分担者 京都産業大学シニアリサーチフェロー）

1.

Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito
Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing
Proc. Natl. Acad. Sci. USA 113 (2016)  doi:10.1073/pnas.1520560113
http://www.pnas.org/content/early/2016/01/27/1520560113.abstract

広報記事
タンパク質合成過程における「緩急のリズム」を実証 -大腸菌遺伝子産物中間状態を網羅的に解析-
http://www.kyoto-su.ac.jp/news/20160205_345_release_ka02.html
http://www.titech.ac.jp/news/2016/033388.html
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船津 高志（東京大学・大学院薬学系研究科 教授）

1. Kazuki Nakamura, Ryo Iizuka, Shinro Nishi, Takao Yoshida, Yuji Hatada, Yoshihiro Takaki, Ayaka Iguchi, Dong Hyun Yoon, Tetsushi Sekiguchi, Shuichi Shoji, Takashi Funatsu.
Culture-independent method for identification of microbial enzyme-encoding genes by activity-based single-cell sequencing using a water-in-oil microdroplet platform.
Sci. Rep. 6: 22259 (2016). doi: 10.1038/srep22259
2. Ryo Iizuka, Takashi Funatsu
【Review】Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins Biophys.
Physicobiol. 13: 63-69 (2016). doi: 10.2142/biophysico.13.0_63
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川口 寧（東京大学医科学研究所 感染・免疫部門 ウイルス病態制御分野 教授）

1. A. Kato, T. Ando, S. Oda, M. Watanabe, N. Koyanagi, J. Arii and Y. Kawaguchi
Roles of Us8A and its phosphorylation mediated by Us3 in herpes simplex virus 1 pathogenesis.
J. Virol. (in press)
2. Y. Sato, A. Kato, Y. Maruzuru, M. Oyama, H. Kozuka-Hata, J. Arii and Y. Kawaguchi
Cellular Transcriptional Coactivator RanBP10 and Herpes Simplex Virus 1 ICP0 Interact and Synergistically Promote Viral Gene Expression and Replication.
J. Virol. 90: 3173-3186. (2016)
3. K. Shindo, A. Kato, N. Koyanagi, H. Sagara, J. Arii, and Y. Kawaguchi
Characterization of a chimera herpes simplex virus 1 (HSV-1) in which its Us3 protein kinase gene was replaced with the HSV-2 Us3 gene.
J. Virol. 90:457-473
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秋山 芳展（京都大学・ウイルス研究所 教授）

1. Miyazaki, R., Yura, T., Suzuki, T., Dohmae, N., Mori, M., and Akiyama, Y.
A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32.
Sci. Rep. 6, 24147 (2016)
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佐藤 明子（広島大学・大学院総合科学研究科 准教授）

1. Satoh, T., Nakamura, Y and Satoh, A. K.
Rab6 functions in polarized transport in Drosophila photoreceptors.
Fly in press (2016)
2. 佐藤卓至・中村祐里・佐藤明子
ショウジョウバエ視細胞の膜タンパク質選別輸送における低分子量Gタンパク質Rab6の役割.　
顕微鏡 51, in press. (2016)
3. Iwanami, N., Nakamura, Y., Satoh, T. and Satoh, A. K.　
Rab6 is required for multiple apical transport pathways but not for basolateral transport pathway in Drosophila photoreceptors.
PLOS Genetics. e1005828.(2016) doi: 10.1371/journal.pgen.1005828
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阪口 雅郎（兵庫県立大学・大学院生命理学研究科 教授）

1.

Yuichiro Kida, Yudai Ishihara, Hidenobu Fujita, Yukiko Onishi, *Sakaguchi, M.
Stability and flexibility of marginally hydrophobic segments stalling at the endoplasmic reticulum translocon.

Mol. Biol. Cell 27: 930-940 (2016). doi: 10.1091/mbc.E15-09-0672
2.

Haruka Sakaue, Shohei Iwashita, Yukari Yamashita, Yuichiro Kida, *Sakaguchi, M.
The N-terminal motif of PMP70 suppresses cotranslational targeting to the endoplasmic reticulum.

J. Biochem. 159: 539-551 (2016). doi: 10.1093/jb/mvv132
3.

Kongsoo Kang, Michiyo Takahara, Haruka Sakaue, *Sakaguchi, M.
Capsid protease domain as a tool for assessing protein-domain folding during organelle import of nascent polypeptides in living cells.

J. Biochem. 159: 497-508 (2016). doi: 10.1093/jb/mvv129
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潮田 亮（京都産業大学・総合生命科学部 助教）

1.

Ryo Ushioda, Akitoshi Miyamotod, Michio Inoue, Satoshi Watanabe, Masaki Okumurae, Ken-ichi Maegawa, Kaiku Uegaki, Shohei Fujii, Yasuko Fukuda, Masataka Umitsu, Junichi Takagi, Kenji Inaba, Katsuhiko Mikoshiba and Kazuhiro Nagata
Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5
Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6055-E6063. Epub 2016 Sep 30., doi: 10.1073/pnas.1605818113
http://www.pnas.org/content/113/41/E6055

プレスリリース
ジスルフィド還元酵素ERdj5がSERCA2bのジスルフィド結合を還元することを解明
http://www.kyoto-su.ac.jp/news/20161001_345_kenkyu_masu01.html

報道

産経新聞（2016年10月3日付23面)、京都新聞（2016年10月1日付33面）、共同通信（オンライン）、日経プレスリリース（オンライン）
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伊藤 拓宏（理化学研究所・ライフサイエンス技術基盤研究センター ユニットリーダー）

1. Kashiwagi, K., Shigeta, T., Imataka, H., Ito, T.* and Yokoyama, S.*
Expression, purification, and crystallization of Schizosaccharomyces pombe eIF2B.
J Struct Funct Genomics, 17, 33-38.(2016) DOI: 10.1007/s10969-016-9203-3. (Epub 2016 Mar 29) (* co-corresponding authors)
2. Kashiwagi, K., Takahashi, M., Nishimoto, M., Hiyama, T.B., Higo, T., Umehara, T., Sakamoto, K., Ito, T.* and Yokoyama, S.*
Crystal structure of eukaryotic translation initiation factor 2B.
Nature, 531, 122-125.(2016) DOI: 10.1038/nature16991. (Epub 2016 Feb 22) (* co-corresponding authors)
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2015年の研究業績

田口 英樹（領域代表・東京工業大学・教授）

1. Niwa, T., Sasaki, Y., Uemura, E., Nakamura, S., Akiyama, M., Ando, M., Sawada, S., Mukai, SA., Ueda, T., Taguchi, H., Akiyoshi, K.
Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system.
Sci Rep. 2015 Dec 15;5:18025. doi: 10.1038/srep18025.
2. T, Niwa., K, Fujiwara., Taguchi, H.
Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach.
FEBS Lett., in press
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今高 寛晃（兵庫県立大学・大学院工学研究科　教授）

1. Machida K and *Imataka H
Production methods of virus particles.
Biotechnology Letters 37: 753-760 (2015) doi: 10.1007/s10529-014-1741-9
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稲田 利文（東北大学・大学院薬学研究科・教授）

1. Tsuboi, T., Yamazaki, R., Nobuta, R., Ikecuhi, K., Makino, S., Ohtaki, Y., Suzuki, Y., Yoshihisa, T., Trotta, C. and *Inada, T.
The tRNA Splicing Endonuclease Complex Cleaves the Mitochondria-localized CBP1 mRNA. 
J Biol. Chem. (2015)
2. Makino, S., Mishima, Y., Inoue, K. and *Inada, T. 
Roles of mRNA-fate modulators Dhh1 and Pat1 in TNRC6-dependent gene silencing recapitulated in yeast. 
J Biol. Chem. (2015)
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岩川 弘宙（東京大学・定量生命科学研究所・助教）

Trends in Cell Biology
1.

  1. Hiro-oki Iwakawa, Yukihide Tomari
    【Review】The Functions of MicroRNAs: mRNA Decay and Translational Repression
      25(11), 651-665(2015)
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田中 元雅（独立行政法人理化学研究所 脳科学総合研究センター　チームリーダー）

1. Suzuki, G., Weissman, J.S., Tanaka, M.
[KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis
Molecular Cell, 60, 651-660 (2015), doi: 10.1016/j.molcel.2015.10.020
プレスリリース（日本語の解説）：http://www.riken.jp/pr/press/2015/20151120_1/
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河野　憲二（奈良先端科学技術大学院大学・バイオサイエンス研究科　教授）

1. *Hirai, S., Kurashima, H., Nakamura, D., Komatsu, T., Yasuda, Y., Habashita-Obata, S., Ichikawa, S., Katsuta, O., Iwawaki, T., Kohno, K.
2-Phenyl-APB-144-induced retinal pigment epithelium degeneration and its underlying mechanisms.
J. Ocul. Pharmacol. Ther., 31, 570-584, (2015)
2. Mathuranyanon, R., Tsukamoto, T., Takeuchi, A., Ishiwata-Kimata, Y., Tuchiya, Y., Kohno, K., *Kimata, Y.
Tight regulation of the unfolded 1 protein sensor Ire1 by its intramolecularly antagonizing subdomain.
J. Cell Sci. 128(9), 1762-1772 (2015)
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藤木　幸夫（九州大学生体防御医学研究所　特任教授）

1. Yoshida, Y., Niwa, H., Honsho, M., Itoyama, A., and Fujiki, Y.
Pex11p mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biology Open, 4, 710-721 (2015).
2. Fujiki, Y., Okumoto, K., and Honsho, M.
Protein import into peroxisomes: the principles and methods of studying (version 2.0).
eLS., pp.1-7 (2015). doi: 10.1002/9780470015902.a0002618.pub2
3. Honsho, M., Abe, Y., and Fujiki, Y.
Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis.
J. Biol. Chem. 290, 28822-28833 (2015).
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千葉 志信（計画研究代表者 京都産業大学・准教授）

1.

Sohmen, D., Chiba, S., Shimokawa-Chiba, N., Innis, A., Berninghausen, O., Beckmann, R., Ito, K. and *Wilson, D.
Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling.
Nat. Commun. (2015)
2.

Shimokawa-Chiba, N., Kumazaki, K., Tsukazaki, T., Nureki, O., Ito, K. and *Chiba, S.
A hydrophilic microenvironment required for the channel-independent insertase function of YidC.

Proc. Natl. Acad. Sci. USA. (2015)
3.
  1. *Chiba, S. and Ito, K.
    MifM monitors total YidC activities of Bacillus subtilis including that of YidC2, the target of regulation.
    J Bacteriol. 197, 99-107 (2015)
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伊藤 維昭（研究分担者 京都産業大学シニアリサーチフェロー）

1.

Sohmen, D., Chiba, S., Shimokawa-Chiba, N., Innis, A., Berninghausen, O., Beckmann, R., Ito, K. and *Wilson, D.
Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling.
Nat. Commun. (2015)
2.

Shimokawa-Chiba, N., Kumazaki, K., Tsukazaki, T., Nureki, O., Ito, K. and *Chiba, S.
A hydrophilic microenvironment required for the channel-independent insertase function of YidC.

Proc. Natl. Acad. Sci. USA. (2015)
3.

*Chiba, S. and Ito, K.
MifM monitors total YidC activities of Bacillus subtilis including that of YidC2, the target of regulation.

J Bacteriol. 197, 99-107 (2015)
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秋山 芳展（京都大学・ウイルス研究所 教授）

1.

Akiyama, K.a, Mizuno, S.a, Hizukuri, Y., Mori, H., Nogi, T., and *Akiyama, Y.
Role of membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage.
eLife 4, e08928(2015)
a equally contributed

2.

 Ishii, E., Chiba, S., Hashimoto, N., Kojima, K., Homma, M., Ito, K., Akiyama, Y., and *Mori, H.  
Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria. 
 Proc. Natl. Acad. Sci. USA in press (2015)
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岡本 浩二（大阪大学・大学院生命機能研究科 准教授）

1. Sakakibara, K., Eiyama, A., Suzuki, S.W., Sakoh-Nakatogawa, M., Okumura, N., Tani, M., Hashimoto, A., Nagumo, S., Kondo-Okamoto, N., Kondo-Kakuta, C., Asai, E., Kirisako, H., Nakatogawa, H., Kuge, O., Takao, T., Ohsumi, Y., and *Okamoto, K.
Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recycling.
EMBO J. in press (2015) PMID: 26438722
2.

Eiyama, A., and *Okamoto, K.
Protein N-terminal acetylation by NatA is critical for selective mitochondria degradation.
J. Biol. Chem. in press (2015) PMID: 26296886

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川口 寧（東京大学医科学研究所 感染・免疫部門 ウイルス病態制御分野 教授）

1. K. Shindo, A. Kato, N. Koyanagi, H. Sagara, J. Arii, and *Kawaguchi, Y.
Characterization of a chimera herpes simplex virus 1 (HSV-1) in which its Us3 protein kinase gene was replaced with the HSV-2 Us3 gene.
J. Virol. 90:457-473 (2015)
2. Z. Liu, A. Kato, M. Oyama, H. Kozuka-Hata, J. Arii, and *Kawaguchi, Y.
Role of Host Cell p32 in Herpes Simplex Virus 1 De-envelopment During Viral Nuclear Egress. 
J. Virol. 89: 8982-8998.(2015)
3. Y. Hirohata, J. Arii, Z. Liu, K. Shindo, M. Oyama, H. Kozuka-Hata, H. Sagara, A. Kato, and *Kawaguchi, Y.
Herpes simplex virus 1 recruits CD98 heavy chain and β1 integrin to the nuclear membrane for viral de-envelopment. 
J. Virol. 89: 7799-7812.(2015)
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伊野部 智由（富山大学・先端ライフサイエンス拠点 特命助教）

1. *Inobe, T. and Genmei, R.
Inhibition of the 26S proteasome by peptide mimics of the coiled-coil region of its ATPase subunits.
Biochem. Biophys. Res. Commun. 468, 143-150 (2015)
2. *Inobe, T., Nozaki, M. and Nukina, N.
Artificial regulation of p53 function by modulating its assembly.
Biochem. Biophys. Res. Commun. 467, 322-327 (2015)
3. Takahashi, K., Matouschek, A. and *Inobe, T.
Regulation of proteasomal degradation modulating an unstructured proteasomal initiation region of a substrate.
ACS Chem. Biol.10, 2537–2543 (2015)
4. Inobe, T. and Genmei, R.
N-terminal coiled-coil structure of ATPase subunits of 26S proteasome is crucial for proteasome function.
PLoS ONE, 10, e0134056 (2015)
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佐藤 明子（広島大学・大学院総合科学研究科 准教授）

1. Satoh, T., Ohba, A., Liu, Z., Inagaki, T., and *Satoh, A.K.
EMC is essential for biosynthesis of rhodopsin and other multipass membrane proteins in Drosophila melanogaster.
eLife, 4, e06306 (2015)
2. 佐藤卓至・佐藤明子
EMCは複数膜貫通ドメイン膜タンパク質の合成に特異的な因子である.
生化学87, 870781. (2015)
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西頭 英起（宮崎大学・医学部機能生化学 教授）

1.

Kadowaki, H., Nagai, A., Maruyama, T., Takami, Y., Satrimafitrah, P., Kato, H., Honda, A., Hatta, T., Natsume, T., Sato, T., Kai, H., Ichijo, H. and *Nishitoh, H.
Preemptive quality control protects the ER from protein overload via the proximity of ERAD components and SRP.
Cell Rep. 13, 944–956 (2015)
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吉久 徹（兵庫県立大学・生命理学研究科 教授）

1. Yoshihisa, T.
Nucleocytoplasmic shuttling of tRNAs and implication of the cytosolic Hsp70 system in tRNA import.
Nucleus, 6(5):339-343 (2015)
2.

Takano, T., Kajita, T., Mochizuki, M., Endo, T., and *Yoshihisa, T.
Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.
eLife, 4, e04659 (2015)
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森戸 大介（京都産業大学・総合生命科学部 主任研究員）

1. Kotani Y, *Morito D, Yamazaki S, Ogino K, Kawakami K, Takashima S, *Hirata H, *Nagata K.
Neuromuscular regulation in zebrafish by a large AAA+ ATPase/ubiquitin ligase, mysterin/RNF213.
Sci Rep. 2015 Nov 4;5:16161
2. Morito D, *Nagata K.
【Review】Pathogenic Hijacking of ER-Associated Degradation: Is ERAD Flexible?
Mol Cell. 2015 Aug 6;59(3):335-44
3.

Kirstein-Miles J#*, Morito D#, Kakihana T#, Sugihara M, Minnen A, Hipp MS, Nussbaum‐Krammer C, *Hartl FU, *Nagata K, and *Morimoto RI
#equally-contributed; *corresponding
Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments
EMBO J, e201591711 (2015)
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2014年の研究業績

田口 英樹（領域代表・東京工業大学・教授）

1.

Ishimoto, T., Fujiwara, K., Niwa, T., *Taguchi, H.
Conversion of a chaperonin GroEL-independent protein into an obligate substrate.

J. Biol. Chem. 289, 32073-32080 (2014)
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今高 寛晃（兵庫県立大学・大学院工学研究科　教授）

1.

Machida K, Mikami S, Masutani M, Mishima K, Kobayashi T, and *Imataka H
A translation system reconstituted with human factors proves that processing of encephalomyocarditisvirus proteins 2A and 2B occurs in the elongation phase of translation without eukaryotic release factors
J. Biol. Chem. 289: 31960-31971 (2014) doi: 10.1074/jbc.M114.593343
2. Fukao A, Mishima Y, Takizawa N, Oka S, Imataka H, Pelletier J, Sonenberg N, Thoma C, and Fujiwara T
MicroRNAs Trigger Dissociation of eIF4AI and eIF4AII from Target mRNAs in Humans
Mol.Cell 56: 79-89 (2014) doi: 10.1016/j.molcel.2014.09.005
3. Kobayashi T, Machida K, and *Imataka H
Human cell extract-derived cell-free systems for virus synthesis. In: Alexandrov,K. and Johnston,W.A. (Eds.), Methods in Molecular Biology 1118, Cell-free protein synthesis: Methods and Protocols. Humana Press, pp149-156 (2014) doi: 10.1007/978-1-62703-782-2_9
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稲田 利文（東北大学・大学院薬学研究科・教授）

1.

  1. Matsuda, R., Ikecuhi, K., Nomura, S. and *Inada, T.
    Protein quality control systems associated with No-Go and Nonstop mRNA surveillance in yeast.

    Genes Cells 19, 1-12 (2014)
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岩川 弘宙（研究分担者 東京大学・助教）

1.

Fukaya, T.#, Iwakawa, HO.#, Tomari, Y.
MicroRNAs Block Assembly of eIF4F Translation Initiation Complex in Drosophila.

Mol Cell. 56(1), 67-78 (2014)
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稲葉 謙次（計画研究代表者 東北大学・教授）

1.

  1. Okumura, M.*, Kadokura, K., Hashimot, S., Yutani, K., Kanemura, S., Hikima, T., Hidaka, Y., Ito, L., Shiba, K., Masui, S., Imai, D., Imaoka, S., Yamaguchi, H.* and Inaba, K.* 
    Inhibition of the functional interplay betweenER oxidoreduclin-1α (Ero1α) and protein disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.
    J. Biol. Chem.289, 27004-27018 (2014).
2.

Kojima, R.†, Okumura, M.†, Masui, S., Kanemura, S., Inoue, M., Saiki, M., Yamaguchi, H., Hikima, T., Suzuki, M., Akiyama, S. and Inaba, K.* (†These authors contributed equally to this work.)
Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide-bond introducer of the mammalian PDI family.
Structure, 22, 431-443 (2014)
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門倉 広（研究分担者 東北大学・准教授）

1.

Okumura, M.*, Kadokura, H., Hashimoto, S., Yutani, K., Kanemura, S., Hikima, T., Hidaka, Y., Ito, L., Shiba, K., Masui, S., Imai, D., Imaoka, S., Yamaguchi, H.* and Inaba, K.*
Inhibition of the functional interplay betweenER oxidoreduclin-1α (Ero1α) and protein disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.
J. Biol. Chem. 289, 27004-27018 (2014).
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河野 憲二（計画研究代表者 奈良先端科学技術大学院大学・教授）

1.

Miyagawa, K, Ishiwata-Kimata, Y., Kohno, K., and *Kimata, Y.  
Ethanol stress impairs protein folding in the endoplasmic reticulum and activates Ire1 in Saccharomyces cerevisiae. 

Biosci. Biotechnol. Biochem. 78(8), 1389-1391 (2014)
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藤木　幸夫（九州大学生体防御医学研究所　特任教授）

1.

Jiang, L., Hara-Kuge, S., Yamashita, S., and Fujiki, Y.
Peroxin Pex14p is the key component for coordinated autophagic degradation of mammalian peroxisomes by direct binding to LC3-II.
Genes Cells 20, 36-49 (2014).
2.

Tamura, S., Matsumoto, N., Takeba, R., and Fujiki, Y.
AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import.
J. Biol. Chem. 289, 24336-24346 (2014).

3.

Miyauchi-Nanri, Y., Mukai, S., Kuroda, K., and Fujiki, Y.
Cul4A-DDB1-Rbx1 E3 ligase controls the quality of the PTS2 receptor Pex7p.
Biochem. J. 463, 65-74 (2014).

4.

Fujiki, Y., Okumoto, K., Mukai, S., Honsho, M., and Tamura, S.
Peroxisome biogenesis in mammalian cells.
Front. Physiol., 5, article 307 (2014).

5.

Yamashita, S., Abe, K., Tatemichi, Y., and Fujiki, Y.
The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy.
Autophagy 10, 1549-1564 (2014).

6.

Noguchi, M., Honsho, M., Abe, Y., Toyama, R., Niwa, H., Sato, Y., Ghaedi, K., Rahmanifar, A., Shafeghati, Y., and Fujiki, Y.
Mild reduction of plasmalogens causes rhizomelic chondrodysplasia punctata: Functional characterization of a novel mutation.
J. Hum. Genet. 59, 387-392 (2014).

7.

Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S.
Molecular basis for peroxisome biogenesis disorders.
In: Molecular Machines Involved in Peroxisomes Maintenance, Berlin, Springer-Verlag, pp. 91-110 (2014).

8.

Fujiki, Y., Itoyama, A., Abe, Y., and Honsho, M.
Molecular complex coordinating peroxisome morphogenesis in Mammalian Cells.
In: Molecular Machines Involved in Peroxisomes Maintenance, Berlin, Springer-Verlag, pp. 391-401 (2014).

9.

Okumoto, K., Noda, H., and Fujiki, Y.
Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1)-receptor Pex5p regulate PTS1 protein import.
J. Biol. Chem. 289: 14089-14108 (2014).
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千葉 志信（計画研究代表者 京都産業大学・准教授）

1.

  1. Nakamori, K., Chiba, S. and *Ito, K.
    Identification of a SecM segment required for export-coupled release from elongation arrest.
    FEBS Lett. 588, 3098-3103 (2014)

2.

Kumazaki, K†., Chiba, S†., Takemoto, M., Furukawa, A., Nishiyama, K.I., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., *Tsukazaki, T. and *Nureki, O.
Structural basis of Sec-independent membrane protein insertion by YidC.

Nature, 509, 516-52 (2014)
(†These authors contributed equally to this work)
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伊藤 維昭（研究分担者 京都産業大学シニアリサーチフェロー）

1.
  1. Nakamori, K., Chiba, S. and *Ito, K.
    Identification of a SecM segment required for export-coupled release from elongation arrest.
    FEBS Lett. 588, 3098-3103 (2014)
2.

Kumazaki, K†., Chiba, S†., Takemoto, M., Furukawa, A., Nishiyama, K.I., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., *Tsukazaki, T. and *Nureki, O.
Structural basis of Sec-independent membrane protein insertion by YidC.
Nature, 509, 516-52 (2014)
(†These authors contributed equally to this work)

3.

*Mio K, Tsukazaki T, Mori H, Kawata M, Moriya T, Sasaki Y, Ishitani R, Ito K, *Nureki O and *Sato C.
Conformational variation of the translocon enhancing chaperone SecDF.
J Struct Funct Genomics. 15, 107-15 (2014)
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これまでの研究業績

田口 英樹（領域代表・東京工業大学・教授）

1.

Ohta, S., Kawai-Noma, S., Kitamura, A., Pack, C-G., *Kinjo, M. & *Taguchi, H.
The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy.

Biochem. Biophys. Res. Commun. in press (2013)
2.

Biswas, S., Kinbara, K., Niwa, T., *Taguchi, H., Ishii, N., Watanabe, S., Miyata, K., Kataoka, K. and *Aida, T.
Biomolecular Robotics for Chemomechanically Driven Guest Delivery Fueled by Intracellular ATP.

Nature Chemistry 5, 613-620 (2013)
3.

*Nojima, T., Konno, H., Kodera, N., Seio, K., *Taguchi, H. and Yoshida, M.
Nano-scale alignment of proteins on a flexible DNA back-bone.

PLoS ONE 7, e52534 (2012)
4.

Nojima, T., Ikegami, T., *Taguchi, H. and *Yoshida, M.
Flexibility of GroES mobile loop is required for efficient chaperonin function.

J. Mol. Biol. 422, 291-299 (2012)
5.

Niwa, T., Kanamori, T., *Ueda, T., and *Taguchi, H.
Global Analysis of Chaperone Effects Using a Reconstituted Cell-Free Translation System.

Proc. Natl. Acad. Sci. USA. 109, 8937-8942 (2012)
6.

Tsuji, T., Kawai-Noma, S., Pack, C.-G., Terajima, H., Yajima, J., Nishizaka, T., Kinjo, M., and *Taguchi, H.
Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells. Biochem. Biophys.

Res. Commun. 405, 638-643 (2011)
7.

*Takemoto K, Niwa T, Taguchi, H.
Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement.

BMC Syst Biol. 5, 98 (2011)
8.

Kawai-Noma, S., Pack, C.-G., Kojidani, T., Asakawa, H., Hiraoka, Y., Kinjo, M., Haraguchi, T., *Taguchi, H., and Hirata, A.
In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

J. Cell Biol. 190, 223-231 (2010)
9.

Fujiwara, K., Ishihama, Y., Nakahigashi, K., Soga, T., and *Taguchi, H.
A systematic survey of in vivo obligate chaperonin-dependent substrates.

EMBO J. 29, 1552-1564 (2010)
10.

*Taguchi, H., and Kawai-Noma, S.
Diffuse oligomer-based transmission of yeast prions. (Review).

FEBS J. 277, 1359-1368 (2010)
11.

Kawai-Noma, S., Pack, C.-G., Tsuji, T., Kinjo, M., and *Taguchi, H.
Single mother-daughter pair analysis to analyze the diffusion properties of yeast prion Sup35 in guanidine-HCl treated [PSI+] cells.

Genes Cells 14, 1045-1054 (2009)
12.

Niwa, T., Ying, B.-W., Saito, K., Jin, W. Z., Takada, S., *Ueda, T., and *Taguchi, H.
Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins.

Proc. Natl. Acad. Sci. USA. 106, 4201-4206 (2009)
13.

Koike-Takeshita, A., Yoshida, M., and *Taguchi, H.
Revisiting the GroEL-GroES reaction cycle via the symmetrical intermediate implied by novel aspects of the GroEL (D398A) mutant.

J. Biol. Chem. 283, 23774-23781 (2008)
14.

Ying, B.-W. *Taguchi, H., *Ueda, T.
Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding.

J. Biol. Chem. 281, 21813-21819 (2006)
15.

Ying, B.-W. Taguchi, H., Kondo, M., *Ueda, T.
Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides.

J. Biol. Chem. 280, 12035-12040 (2005)
16.

Ueno, T.#, Taguchi, H.#, Tadakuma, H., *Yoshida, M., and *Funatsu, T. [# equally contributed]
GroEL mediates protein folding with a two successive timer mechanism.

Mol. Cell 14, 423-434 (2004)
17.

Taguchi, H., Ueno, T., Tadakuma, H., *Yoshida, M., and *Funatsu, T.
Single-molecule observation of protein-protein interactions in the chaperonin system.

Nat. Biotechnol. 19, 861-865 (2001)
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今高 寛晃（研究分担者 兵庫県立大学・教授）

1.

Masutani, M., Machida, K., Kobayashi, T., Yokoyama, S. and *Imataka, H.
Reconstitution of eukaryotic translation initiation factor 3 by co-expression of the subunits in a human cell-derived in vitro protein synthesis system.

Protein Expr. Purif. 87, 5-10 (2013)
2.

Machida, K., Masutani, M., Kobayashi, T., Mikami, S., Nishino, Y., Miyazawa A. and *Imataka, H.
Reconstitution of the human chaperonin CCT by co-expression of the eight distinct subunits in mammalian cells.

Protein Expr. Purif. 82, 61-69 (2012)
3.

Masutani, M., Sonenberg, N., Yokoyama, S. and *Imataka, H.
Reconstitution reveals the functional core of mammalian eIF3.

EMBO J. 26, 3373-3383 (2007)

富田（竹内） 野乃（計画研究分担者 東京大学・准教授）

1.

Kotani T., Akabane S., Takeyasu K., Ueda T. and *Takeuchi N.
Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial ribosome subunit and are involved in translation and assembly of respiratory complexes.

Nucleic Acids Res. 41, 3713-22 (2013)
2.

Suematsu T., Yokobori SI., Morita H., Yoshinari S., Ueda T., Kita K., *Takeuchi N., Watanabe YI.
A bacterial elongation factor G homolog exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi.

Mol Microbiol. 75, 1445 - 1454 (2010)
3.

Akama K., Christian BE., Jones CN., *Takeuchi N., and Spremulli LL.
Analysis of the Functional Consequences of Lethal Mutations in Mitochondrial Translational Elongation Factors.

Biochimica et Biophysica Acta 1802, 692-698 (2010)
4.

Tsuboi M., Morita H.,Nozaki Y.,Akama K., Ueda T.,Ito K.,Nierhaus KH., and *Takeuchi N.
EF-G2mt is an Exclusive Recycling Factor in Mammalian Mitochondrial Protein Synthesis.

Mol. Cell 28, 502-10 (2009)
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稲田 利文（計画研究代表者 東北大学・教授）

1.

Kuroha, K., Ando, K., Nakagawa, R., *Inada, T.
The Upf complex interacts with aberrant products derived from mRNAs containing a premature termination codon and facilitates their proteasomal degradation.

J Biol. Chem. doi: 10.1074/jbc.M113.460691 (2013)
2.

Tsuboi, T., Kuroha, K., Kudo, K., Makino S., Inoue, E., Kashima, I. and *Inada, T.
Dom34:Hbs1 Plays a General Role in Quality Control Systems by Dissociation of Stalled Ribosome at 3’ End of Aberrant mRNA.

Mol. Cell 26, 518-529 (2012)
3.

Izawa, T., Tsuboi, T., Kuroha, K., Inada, T., Nishikawa, SI., *Endo, T.
Roles of Dom34:Hbs1 in Nonstop Protein Clearance from Translocators for Normal Organelle Protein Influx.

Cell Reports 2, 447-453. (2012)
4.

Brandman, O., Ornstein, JS., Wong, D., Larson, A., Williams, C.C, Li, G.W., Zhou, S., King, D., Shen, P.S, Weibezahn, J., Dunn, J.G, Rouskin, S., Inada, T., Frost, A., *Weissman, JS.
A ribosome-bound quality controlcomplex triggers nascent peptides and signals translation stress.

Cell 151, 1042-1054 (2012)
5.

Kobayashi, K., Kikuno, I., Kuroha, K., Saito, K., Ito, K., Ishitani, R., Inada, T. and *Nureki, O.
Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex.

Proc. Natl. Acad. Sci. USA 107, 17575-17579 (2010)
6.

Kuroha, K., Akamatsu, M., Dimitrova, L., Ito, T., Kato, Y. Shirahige, K. and *Inada, T.
RACK1 stimulates nascent polypeptide-dependent translation arrest.

EMBO Reports 11, 956-961 (2010)
7.

Kuroha, K., Tatematsu, T. and *Inada, T.
Upf1p stimulates proteasome-mediated degradation of the product derived from the specific nonsense-containing mRNA.

EMBO Reports 10, 1265-1271 (2009)
8.

Kuroha, K., Dimitrova, L., Tatematsu, T. and *Inada, T.
Nascent peptide-dependent translation arrest leads to not4p-mediated protein degradation by the proteasome.

J. Biol. Chem. 284, 10343-10352 (2009)
9.

Nukazuka, A., Fujisawa, H., Inada, T., Oda, Y., *Takagi, S.
Semaphorin controls epidermal morphogenesis by stimulating mRNA translation via eIF2 in Caenorhabditis elegans.

Genes Dev. 22, 1025-1036 (2008)
10.

Ito-Harashima, S., Kuroha, K., Tatematsu, T. and *Inada, T.
Translation of poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast.

Genes Dev. 21, 519-524 (2007)
11.

*Inada, T. and Aiba, H.
Translation of aberrant mRNAs lacking a termination codon or with a shortened 3'-UTR is repressed after initiation in yeast.
EMBO J. 24, 1584-1595 (2005)

12.

Kawamoto, H., Morita, T., Shimizu, A., Inada, T., *Aiba, H.
Implication of membrane localization of target mRNA in the action of a small RNA: mechanism of post-transcriptional regulation of glucose transporter in Escherichia coli.

Genes Dev. 19, 328-338 (2005)
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長尾 翌手可（研究分担者 東京大学・助教）

1.

Chujo, T., Ohira, T., Sakaguchi, Y., Goshima, N., Nomura, N., Nagao, A. and *Suzuki, T.
LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria.

Nucleic Acids Res. 40, 8033-8047 (2012)
2.

Suzuki, T., Nagao, A. and *Suzuki, T.
Human mitochondrial tRNAs: biogenesis, function, structural aspects and diseases.

Annu Rev Genet. 45, 299-329 (2011)
3.

Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and *Nureki, O.
Crystal structure of a novel jmjC-domain-containing protein, TYW5, involved in tRNA modification.
Nucleic Acids Res. 39, 1576-1585 (2011)
4.

Nagao, A., Suzuki, T., Katoh, T., Sakaguchi, Y. and *Suzuki, T.
Biogenesis of glutaminyl-mt tRNAGln in human mitochondria.

Proc. Natl. Acad. Sci. USA. 106, 16209-16214 (2009)
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岩川 弘宙（研究分担者 東京大学・助教）

1.

Iwakawa, HO., *Tomari, Y.
Molecular insights into microRNA-mediated translational repression in plants.

Mol. Cell. 52(4), 591-601.
2.

Endo, Y., *Iwakawa, HO., *Tomari, Y.
Arabidopsis ARGONAUTE7 selects miR390 through multiple checkpoints during RISC assembly.

EMBO Reports 14, 652-8. (2013)
3.

Iwakawa, HO., Tajima, Y., Taniguchi, T., Kaido, M., Mise, K., Tomari, Y., Taniguchi, H., *Okuno, T.
Poly(A)-binding protein facilitates translation of an uncapped/nonpolyadenylated viral RNA by binding to the 3' untranslated region.

J. Virol. 86, 7836-49. (2012)
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田中 元雅（計画研究代表者 独立行政法人理化学研究所 チームリーダー）

1.

Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., *Saido, T.C.
Aβ secretion and plaque formation depend on autophagy.
Cell Reports, in press.
2.

Suzuki, G., *Tanaka, M.
Active conversion to the prion state as a molecular switch for cellular adaptation to environmental stress.

Bioessays 35, 12-16 (2013)
3.

Suzuki, G. Shimazu, N., and *Tanaka, M.
A Yeast Prion, Mod 5, Promotes Acquired Drug Resistance and Cell Survival Under Environmental Stress.
Science 336, 355-359 (2012)
4.

*Tanaka, M.
Tracking a toxic polyglutamine epitope.
Nat. Chem. Biol. 7, 861-862 (2011)
5.

Foo, C.K., Ohhashi, Y., Kelly, M.J., Tanaka, M., and *Weissman, J.S.
Radically Different Amyloid Conformationshimeric Sup35 Prion.
J. Mol. Biol. 408, 1-8 (2011)

6.

Ohhashi, Y., Ito, K., Toyama, B.H., Weissman, J.S., and *Tanaka, M.
Differences in prion strain conformations result from non-native interactions in a nucleus.
Nat. Chem. Biol. 6, 225-230 (2010)
7.

Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., and *Tanaka, M.
Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity.
Proc. Natl. Acad. Sci. USA 106, 9678-9684 (2009)

8.

Krzewska, J., Tanaka, M., Burston, S.G., and *Melki, R.
Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain.
J. Biol. Chem. 282, 1679-1686 (2007)
9.

Tanaka, M., Collins, S.R., Toyama, B.H., and *Weissman, J.S.
The Physical Basis of How Prion Conformations Determine Strain Phenotypes.

Nature 442, 585-589 (2006)
10.

Tanaka, M., Chien, P., Yonekura, K., *Weissman, J.S.
Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins.

Cell 121, 49-62 (2005)
11.

Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N.R., Doi, H., Kurosawa, M., Nekooki, M., and *Nukina, N.
Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease.
Nat. Med. 10, 148-154 (2004)

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稲葉 謙次（計画研究代表者 東北大学・教授）

1.

Sato, Y., Kojima, R., Okumura, M., Hagiwara, M., Masui, S., Maegawa, K., Saiki, M., Horibe, T., Suzuki, M. and *Inaba, K.
Synergistic cooperation of PDI family member proteins in peroxiredoxin 4-driven oxidative protein folding.

Sci. Rep. 3, 2456 (2013)
2.

Vavassori, S., Cortini, M., Masui, S. Sannino, S., Anelli, T., Caserta, I. R., Fagioli, C., Fornili, A., Mossuto, M. F., Degano, M, Inaba, K. and *Sitia, R.
A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly.
Mol. Cell 50, 783-792 (2013)

3.

Sato, Y. and *Inaba, K.
Disulfide bond formation network in the biological kingdoms. (Review)
FEBS J. 279, 2262-2271 (2012)

4.

Araki, K., and *Inaba, K.
Structure, mechanism and evolution of Ero1 family enzymes. (Review)

Antioxid. Redox Signal. 16, 790-799 (2012)
5.

Masui, S., Vavassori, S., Fagioli, C., Sitia, R., and *Inaba, K.
Molecular bases of cyclic and specific disulfide interchange between human Ero1a protein and protein-disulfide isomerase (PDI).
J. Biol. Chem. 286, 16262-16271 (2011)
6.

Hagiwara, M., Maegawa, K., Suzuki, M., Ushioda, R., Araki, K., Matsumoto, Y., Hoseki, J., *Nagata, K., and *Inaba, K.
Structural basis of an ERAD pathway mediated by the ER-resident disulfide reductasse ERdj5.
Mol. Cell 41, 432-444 (2011)
7.

*Inaba, K., Masui, S., Iida, H., Vavassori, S., Sitia, R., and Suzuki, M.
Crystal structures of human Ero1a reveal the mechanisms of regulated and targeted oxidation of PDI.
EMBO J. 29, 3330-3343 (2010)
8.

*Inaba, K., Murakami, S., Nakagawa, A., Iida, H., Kinjo, H., Ito, K., and Suzuki, M.
Dynamic nature of disulfide bond formation catalysts revealed by crystal structures of DsbB.
EMBO J. 28, 779-791 (2009)
9.

*Inaba, K., Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K., and *Ito, K.
Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.

Cell 127, 789-801 (2006)
10.

Inaba, K., Takahashi, Y.-H., *Ito, K., and *Hayashi, S.
Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. Proc.

Natl. Acad. Sci. USA 103, 287-292 (2006)
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門倉 広（研究分担者 東北大学・准教授）

1.

*Kadokura, H., Saito, M., Tsuru, A., Hosoda, A., Iwawaki, T., Inaba, K., and *Kohno, K.
Identification of the redox partners of ERdj5 /JPDI, a PDI family member, from an animal tissue.
Biochem. Biophys. Res. Commun. in press (2013)
2.

Chng, S.S., Xue, M., Garner, R.A., Kadokura, H., Boyd, D., Beckwith, J., and *Kahne, D.
Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export.
Science 337, 1665-1668 (2012)
3.

Yanagitani, K., Kimata, Y., Kadokura, H., and *Kohno, K.
Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA.

Science 331, 586-589 (2011)
4.

*Kadokura, H., and *Beckwith, J.
Detecting folding intermediates of a protein as it passes through the bacterial translocation channel.

Cell 138, 1164-1173 (2009)
5.

Kadokura, H., Tian, H., Zander, Bardwell, J.C.A., and *Beckwith, J.
Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding.

Science 303, 534-537 (2004)
6.

Kadokura, H., and *Beckwith, J.
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
EMBO J. 21, 2354-2363 (2002)
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河野 憲二（計画研究代表者 奈良先端科学技術大学院大学・教授）

1.

*Kadokura H., Saito, M., Tsuru, A., *Kohno, K.（7人中7番目）
Identification of the redox partners of ERdj5/JPDI, a PDI family member, from an animal tissue.

Biochem. Biophys. Res. Commun., in press (2013)
2.

Adolph, T.E., Kohno, K., *Blumberg, R.S.（25人中13番目）
Paneth cells as a site of origin for intestinal inflammation.

Nature, in press (2013)
3.

Tsuru, A., Saito, M., Ron, D., *Kohno, K.（10人中10番目）
Negative feedback by IRE1β optimizes mucin production in goblet cells.

Proc. Natl. Acad. Sci. USA 110, 2864-2869 (2013)
4.

Shinya, S., Yanagitani, K., *Kohno, K.（人中6番目）
Reconstitution and characterization of the unconventional slicing of XBP1u mRNA in vitro.

Nucleic Acids Res. 39, 5245-5254 (2011)
5.

Yanagitani, K., Kimata, Y., Kadokura, H. *Kohno, K.
Translational pausing ensures membrane-targeting and cytoplasmic splicing of XBP1u mRNA.

Science 331, 586-589 (2011)
6.

Promlek, T., Ishiwata-Kimata, Y., Shido, M., Sakuramoto, M., Kohno, K. *Kimata, Y.
Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum-stress sensor Ire1 in different ways.

Mol. Biol. Cell 22, 3520-3532 (2011)
7.

Kimata, Y., *Kohno, K.
Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells.（Review）

Curr. Opin. Cell Biol. 23, 135-142 (2011)
8.

Nakamura, D., Tsuru, A., Imagawa, Y., *Kohno, K.（6人中6番目）
Mammalian ER stress sensor IRE1β specifically down-regulates the synthesis of secretory pathway proteins.

FEBS Lett. 585, 133-138 (2011)
9.

Yamamoto, Y.H., Kadokura, H., *Kohno, K.（8人中8番目）
A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR.

Cell Struct. Funct. 35, 107-116 (2010)
10.

*Iwawaki, T., Akai, R., Yamanaka, S., Kohno, K.
Function of IRE1alpha in the placenta is essential for placental development and embryonic viability.

Proc. Natl. Acad. Sci. USA 106, 16657-16662 (2009)
11.

Yanagitani, K., Imagawa, Y., Iwawaki, T., Hosoda, A., Saito, M., Kimata, Y., *Kohno, K.
Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA.

Mol. Cell 34, 191-200 (2009)
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藤木 幸夫（計画研究代表者 九州大学・教授）

1.

Honsho, M., Asaoku, S., Fukumoto, K., and *Fujiki, Y.
Topogenesis and homeostasis of fatty acyl-CoA reductase 1.

J. Biol. Chem., in press (2013)
2.

Yagita, Y., Hiromasa,T., and *Fujiki, Y.
Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway.

J. Cell Biol. 200, 651-666 (2013)
3.

Otera, H., and *Fujiki, Y.
Pex5p imports folded tetrameric catalase by interaction with Pex13p.

Traffic 13, 1364-1377 (2012)
4.

*Fujiki, Y., Yagita, Y., and Matsuzaki, T.
Peroxisome biogenesis disorders: molecular basis for impaire peroxisomal membrane assembly.
Biochim. Biophys. Acta- Mol. Basis Dis. 1822, 1337-1342 (2012)
5.

Itoyama, A., Honsho, M., Abe, Y., Moser, A., Yoshida, Y., and *Fujiki, Y.
Docosahexaenoic acid mediates peroxisomal elongation, a prerequisite for peroxisome division.

J. Cell Sci. 125, 589-602 (2012)
6.

Miyata, N., Okumoto, K., Noguchi, M., Mukai, S., and *Fujiki, Y.
AWP1/ZFAND6 functions in Pex5 export by interacting with Cys-monoubiquitinated Pex5 and Pex6 AAA ATPase.

Traffic 13, 168-183 (2012)
7.

Yonekawa, S., Furuno, A., Baba, T., Fujiki, Y., Ogasawara, Y., Yamamoto, A., Tagaya, M., and *Tani, K.
Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells.

Proc. Natl. Acad. Sci. USA 108, 12746-12751 (2011)
8.

Okumoto, K., Misono, S., Miyata, N., Matsumoto, Y., Mukai, S., and *Fujiki, Y.
Cysteine-ubiquitination of peroxisome-targeting-signal type 1 (PTS1)-receptor Pex5p regulates Pex5p recycling.

Traffic 12, 1067-1083 (2011)
9.

Matsuzaki, T., and *Fujiki, Y.
The peroxisomal membrane-protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway.

J. Cell Biol. 183, 1275-1286 (2008)
10.

Matsumoto, N., Tamura, S., and *Fujiki, Y.
The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA-ATPase complexes to peroxisomes.

Nature Cell Biol. 5, 454-460 (2003)
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田村 茂彦（研究分担者 九州大学・教授）

1.

Su, J. R., Takeda, K., Tamura, S., *Fujiki., Y., and *Miki, K.
Crystal struture of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p.

Proc. Natl. Acad. Sci. USA 106, 417-421 (2009)
2.

Tamura, S., Yasutake, S., Matsumoto, N., and *Fujiki, Y.
Dynamic and functional assembly of the AAA peroxins, Pex1p, and Pex6p, and their membrane receptor Pex26p.

J. Biol. Chem. 281, 27693-27704 (2006)
3.

Furuki, S., Tamura, S., Matsumoto, N., Miyata, N., Moser, A., Moser, H.W., and *Fujiki, Y.
Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with Pex1p-Pex6p complex.

J. Biol. Chem. 281, 1317-1323 (2006)

千葉 志信（計画研究代表者 京都産業大学・准教授）

1.

*Ito, K. and Chiba, S.
Arrest peptides: cis-acting modulators of translation.

Annu. Rev. Biochem. 82, 171-202 (2013)
2.

Chiba, S., *Ito, K.
Multisite ribosomal stalling: A unique mode of regulatory nascent chain action revealed for MifM.

Mol. Cell 47, 863-872 (2012)
3.

Ito, K., Chadani, Y., Nakamori, K., Chiba, S., Akiyama, Y. and *Abo, Y.
Nascentome analysis uncovers futile protein synthesis in Escherichia coli.

PLoS ONE 6(12), e28413. (2011)
4.

Saito, A., Hizukuri, Y., Matsuo, E. -i., Chiba, S., Mori, H., Nishimura, O., Ito, K. and *Akiyama, Y.
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria.

Proc. Natl. Acad. Sci. USA. 108, 13740-13745 (2011)
5.

Chiba, S., Kanamori, T., Ueda, T., Akiyama, Y., Pogliano, K. and *Ito, K.
Recruitment of a species-specific translational arrest module to monitor different cellular processes.

Proc. Natl. Acad. Sci. USA. 108, 6073-6078 (2011)
6.

White, R., Chiba, S., Pang, T., Dewey, J. S., Savva, C. G., Holzenburg, A., Pogliano, K. and *Young, R.
Holin triggering in real time.

Proc. Natl. Acad. Sci. USA. 108, 798-803 (2011)
7.

Chiba, S., Lamsa, A. and *Pogliano, K.
A ribosome-nascent chain sensor of membrane protein biogenesis in Bacillus subtilis.

EMBO J. 18, 3461-3475 (2009)
8.

Aung, S., Shum, J., Abanes-De, Mello, A., Broder, D. H., Fredlund-Gutierrez, J., Chiba, S. and *Pogliano, K.
Dual localization pathways for the engulfment proteins during Bacillus subtilis sporulation.
Mol. Microbiol. 65, 1534-1546 (2007)
9.

Chiba, S., Coleman, K. and *Pogliano, K.
Impact of membrane fusion and proteolysis on SpoIIQ dynamics and interaction with SpoIIIAH.

J. Biol. Chem. 282, 2576-2586 (2007)

伊藤 維昭（研究分担者 京都産業大学シニアリサーチフェロー）

1.

Chadani, Y., Ito, K., Kutsukake, K. and *Abo T.
ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli.

Mol. Microbiol. 86, 37-50 (2012)
2.

Tsukazaki, T, Mori, H., Echizen, Y., Ishitani, R., Fukai, S., Tanaka, T., Perederina, A., Vassylyev, D. G., Kohno, T., Maturana, A. D., Ito, K., and *Nureki, O.
Structure and function of a membrane component SecDF that enhances protein export.
Nature 474, 235–238 (2011)
3.

Ito, K., Chiba, S. and *Pogliano, K.
Divergent stalling sequences sense and control cellular physiology.
Biochem. Biophys. Res. Commun. 393, 1-5 (2010)
4.

Inaba, K., Murakami, S., Nakagawa, A., Iida, H. Kinjo, M., Ito, K. and *Suzuki, M.
Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB.

EMBO J. 28, 779-791 (2009)