研究業績

2020年

  1. Kori S*, Jimenji T*, Ekimoto T*, Sato M, Kusano F, Oda T, Unoki M, Ikeguchi M, Arita K. (*These authors equally contributed to this work.) Serine 298 phosphorylation in linker 2 of UHRF1 regulates ligand-binding property of its tandem Tudor domain. J. Mol. Biol., in press (2020)
  2. *Nishiyama A, Mulholland C, Bultmann S, Kori S, Endo A, Saeki Y, Qin W, Trummer C, Chiba Y, Yokoyama H, Kumamoto S, Kawakami T, Hojo H, Nagae G, Aburatani H, Tanaka K, *Arita K, *Leonhardt H, and *Nakanishi M. Two distinct modes of DNMT1 recruitment ensure stable maintenance DNA methylation. Nature Communications. 11 Article number:1222. 2020
    DOI: 10.1038/s41467-020-15006-4
  3. Mishima Y, Brueckner L, Takahashi S, Kawakami T, Otani J, Shinohara A, Takeshita K, Garvilles RG, Watanabe M, Sakai N, Takeshima H, Nachtegael C, Nishiyama A, Nakanishi M, Arita K, Nakashima K, Hojo H, Suetake I. Enhanced processivity of Dnmt1 by monoubiquitinated histone H3.Genes to Cells. 25 22-32, 2020.
    DOI: 10.1111/gtc.12732

2019年

  1. Jimenji T., Matsumura R., Kori S. and *Arita K. Structure of PCNA in complex with DNMT1 PIP box reveals the basis for the molecular mechanism of the interaction. Biochemical and Biophysical Research Communications 516, 578-583, 2019
  2. DOI: 10.1016/j.bbrc.2019.06.060
  3. Kori S., Ferry L., Matano S., Jimenji T., Kodera N., Tsusaka T., Matsumura R., Oda T., Sato M.,Dohmae N., Ando T., Shinkai Y., *Defossez PA and *Arita K. Structure of the UHRF1 Tandem Tudor Domain Bound to a Methylated Non-histone Protein, LIG1, Reveals Rules for Binding and Regulation. Structure 27, 485-496, 2019

2017年

  1. *Ishiyama S, *Nishiyama A, Saeki Y, Moritsugu K, Morimoto D, Yamaguchi L, Arai N, Matsumura R, Kawakami T, Mishima Y, Hojo H, Shimamura S, Ishikawa F, Tajima S, Tanaka K, Ariyoshi M, Shirakawa M, Ikeguchi M, Kidera A, **Suetake I, **Arita K, **Nakanishi M. Structure of the Dnmt1 reader module complexed with a unique two-mono-ubiquitin mark on histone H3 reveals the basis for DNA methylation maintenance. Molecular Cell 68 350-360, 2017. Featured articleに選出
    doi: http://dx.doi.org/10.1016/j.molcel.2017.09.037
  2. L. Mishima Y*, Brueckner L*, Takahashi S, Kawakami T, Arita K, Oka S, Otani J, Hojo H, Shirakawa M, Suetake I. RFTS-dependent negative regulation of Dnmt1 by nucleosome. The FEBS Journal 284, 3455-3469 2017 doi: 10.1111/febs.14205
  3. Ferry L*, Fournier A*, Tsusaka T*, Adelmant G, Shimazu T, Matano S, Kirsh O, Amouroux R, Dohmae N, Suzuki T, Filion GJ, Deng W, de Dieuleveult M, Fritsch L, Kudithipudi S, Jeltsch A, Leonhardt H, Hajkova P, Marto JA, Arita K, Shinkai Y**, Defossez PA**. Methylation of DNA Ligase 1 by G9a/GLP recruits UHRF1 to replicating DNA and regulates DNA methylation. Molecular Cell 67, 550-565, 2017 doi: 10.1016/j.molcel.2017.07.012
  4. Yamaguchi L, Nishiyama A, Misaki T, Johmura Y, Ueda J, Arita K, Nagao K, Obuse C, Nakanishi M. Usp7-dependent histone H3 deubiquitylation regulates maintenance of DNA methylation. Sci Rep. 2017 Dec;7(1):55. doi: 10.1038/s41598-017-00136-5.

2016年

  1. Kobayashi T, Obana Y, Kuboi N, Kitayama Y, Hayashi S, Oka M, Wada N, Arita K, Shimizu T, Sato M, Kanaly RA, Kutsuna S. Analysis of the Fine-Tuning of Cyanobacterial Circadian Phase by Monochromatic Light and Long-Day Conditions. Plant Cell Physiol, 57, 105-114, 2016.

2015年

  1. Morimoto D, Walinda E, Fukada H, Sou YS, Kageyama S, Hoshino M, Fujii T, Tsuchiya H, Saeki Y, Arita K, Ariyoshi M, Tochio H, Iwai K, Namba K, Komatsu M, Tanaka K, Shirakawa M. The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates. Nat Commun. 2015 Jan 20;6:6116. 2015. doi: 10.1038/ncomms7116.

2014

  1. Tsutsumi N, Kimura T, Arita K, Ariyoshi M, Ohnishi H, Yamamoto T, Zuo X, Maenaka K, Park EY, Kondo N, Shirakawa M, Tochio H, Kato Z. The structural basis for receptor recognition of human interleukin-18. Nat Commun. 5, 5340- 2014. doi: 10.1038/ncomms6340.
  2. Kimura T, Tsutsumi N, Arita K, Ariyoshi M, Ohnishi H, Kondo N, Shirakawa M, Kato Z, Tochio H. Purification, crystallization and preliminary X-ray crystallographic analysis of human IL-18 and its extracellular complexes. Acta Crystallogr F Struct Biol Commun. 70, 1351-6, 2014. doi: 10.1107/S2053230X14016926.
  3. Berkyurek AC, Suetake I, Arita K, Takeshita K, Nakagawa A, Shirakawa M, Tajima S. The DNA Methyltransferase Dnmt1 Directly Interacts with the SET and RING Finger Associated (SRA) Domain of the Multifunctional Protein Uhrf1 to Facilitate Accession of the Catalytic Center to Hemi-methylated DNA. JBC 289, 379-86, 2014.

2013

  1. Nishiyama A, Yamaguchi L, Sharif J, Johmura Y, Kawamura T, Nakanishi K, Shimamura S, Arita K, Kodama T, Ishikawa F, Koseki H, and Nakanishi M . Uhrf1-dependent ubiquitylation of histone H3 at lysine 23 couples maintenance DNA methylation and DNA replication. Nature 502, 249-253, 2013.
  2. Hori Y, Norinobu T, Sato M, Arita K, Shirakawa M, Kikuchi K. Development of Fluorogenic Probes for Quick No-Wash Live-Cell Imaging of Intracellular Proteins. JACS. 135, 12360-12365, 2013.
  3. Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, Ariyoshi M, Tochio H, Shirakawa M, Hamachi I. Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR. Chem Commun (Camb). 49, 2801-2803, 2013.
  4. Otani J, Arita K, Kato T, Kinoshita M, Kimura H, Suetake I, Tajima S, Ariyoshi M, Shirakawa M. Structural basis of the versatile DNA recognition ability of the methyl CpG binding domain of methyl-CpG binding domain protein 4. J. Biol. Chem. 288, 6351-6362, 2013.
  5. Unoki M, Masuda A, Dohmae N, Arita K, Yoshimatsu M, Iwai Y, Fukui Y, Ueda K, Hamamoto R, Shirakawa M, Sasaki H, Nakamura Y. Lysyl 5-Hydroxylation, a Novel Histone Modification, by Jumonji Domain Containing 6 (JMJD6). J. Biol. Chem. 288, 6053-6062, 2013.

2012

  1. Arita K, Isogai S, Oda T, Unoki M, Sugita K, Sekiyama N, Kuwata K, Hamamoto R, Tochio H, Sato M, Ariyoshi M, Shirakawa M. Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1. Proc Natl Acad Sci U S A. 109, 12950-12955, 2012.

2011

  1. Isogai S, Morimoto D, Arita K, Unzai S, Tenno T, Hasegawa J, Sou YS, Komatsu M, Tanaka K, Shirakawa M, Tochio H. Crystal structure of the UBA domain of p62 and its interaction with ubiquitin. J Biol Chem. 286, 31864-31874, 2011.

2010

  1. Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M., Tochio H., Saitoh H. and Shirakawa M. Structural basis for regulation of poly-SUMO chain by SUMO-like domain of Nip45. Proteins. 78, 1491-1502, 2010.
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それ以前

  1. Otani J., Nankumo T., Arita K., Inamoto S., Ariyoshi M.,and Shirakawa M. Structural basis for recognition of H3K4 methylation status by the DNMT3A ADD domain. Embo Rep. 11, 1235-1241, 2009.
  2. Arita K., Ariyoshi M., Tochio H., Nakamura Y., and Shirakawa M. Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism. Nature. 455, 818-821, 2008.
  3. Arita K., Hashimoto H., Igari K., Akaboshi M., Kutsuna S., Sato M. and Shimizu T. Structural and Biochemical Characterization of a Cyanobacterium Circadian Clock-modifier Protein. J. Biol. Chem. 282, 1128-1135, 2007.
  4. Luo Y., Arita K., Bhatia M., Knuckley B., Lee Y. H., Stallcup M. R., Sato M. and Thompson PR. Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization. Biochemistry. 45, 11727-11736, 2006.
  5. Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M. Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4. Proc Natl Acad Sci U S A. 103, 5291-5296, 2006.
  6. Naoe, Y,. Arita K., Hashimoto, H., Kanazawa, H., Sato, M. and Shimizu, T. Structural characterization of calcineurin B homologous protein 1. J. Biol. Chem. 280, 32372-32378, 2005.
  7. Naoe, Y,. Arita K., Hashimoto, H., Kanazawa, H., Sato, M. and Shimizu, T. Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1. Acta Cryst. F61, 612-613, 2005.
  8. Arita K., Hashimoto, H., Shimizu, T., Nakashima, K., Yamada, M. and Sato, M. Structure basis for Ca2+-induced activation of human PAD4. Nat.Sstruct. & Mol. Biol. 11, 777-783, 2004.
  9. Arita K., Hashimoto, H., Shimizu, T., Yamada, M. and Sato, M. Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase V. Acta Cryst. D59, 2332-2333, 2003.
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日本語総説等

  1. 有田恭平. ヒストンシトルリン化酵素の構造と立体構造に基づく阻害剤の開発. 医学のあゆみ 255, 863-869 2015年(査読なし)
  2.    
  3. 有田恭平. 相関構造生物学によるUHRF1のヒストン認識機構の解明. 日本結晶学会誌 第57巻第1号 P53, 2015年(査読なし)
  4.    
  5. 有田 恭平, 佐藤 衛. カルシウム結合によって活性されるヒストン修飾酵素PAD4の構造科学的基盤. 日本結晶学会誌 47, 268-273, 2005. (査読なし)
  6.    
  7. 有田 恭平, 清水 敏之, 橋本 博, 佐藤 衛. ヒストン修飾酵素Peptidylarginine deimianse 4 (PAD4) の活性化とヒストン認識機構. PF NEWS 24, 16-22, 2006. (査読なし)
  8.    

受賞歴

  1. 平成27年度文部科学大臣賞若手科学者賞(2015年)
  2.    
  3. 第9回日本エピジェネティクス研究会奨励賞受賞 (2015年)
  4.    
  5. 第4回日本エピジェネティクス研究会年会長賞受賞 (2010年)