有田 恭平（アリタ　キョウヘイ）

有田 恭平
学位
理学博士
所属・職位
横浜市立大学 大学院生命医科学研究科
准教授
URL
http://www-mls.tsurumi.yokohama-cu.ac.jp/xtal-mls/
研究分野
構造生物学

原著論文

  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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. 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.
  17. 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.
  18. 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.
  19. 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.
  20. 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.
  21. 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.

総説等

  1. 「相関構造生物学によるUHRF1のヒストン認識機構の解明」有田恭平、日本結晶学会誌　第57巻第1号　P53, 2015年
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