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Structural basis of the substrate specificity of the alpha-tubulin acetyltransferase

Research Project

Project/Area Number 26440033
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Structural biochemistry
Research InstitutionKyushu University

Principal Investigator

Yuzawa Satoru  九州大学, 医学研究院, 共同研究員 (40515029)

Project Period (FY) 2014-04-01 – 2017-03-31
Project Status Completed (Fiscal Year 2016)
Budget Amount *help
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Keywords翻訳後修飾 / 微小管 / 酵素 / 基質特異性 / X線結晶構造解析 / 分子認識 / 酵素反応 / 蛋白質
Outline of Final Research Achievements

The functions of microtubules are controlled in part by tubulin post-translational modification. αTAT1 is the major α-tubulin acetyltransferase in ciliated organisms and acetylates conserved lysine residue at lysine 40 on α-tubulin proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine. In this study, we determined the crystal structures of αTAT1 bound to its substrate acetyl-CoA or CoA and show the cofactor-mediated stabilization of αTAT1.We also elucidate the recognition of α-tubulin by αTAT1 using wild type and mutant proteins and study on structure of the CoA disulfide bound αTAT1.

Report

(4 results)
  • 2016 Annual Research Report   Final Research Report ( PDF )
  • 2015 Research-status Report
  • 2014 Research-status Report
  • Research Products

    (5 results)

All 2017 2015

All Journal Article (3 results) (of which Peer Reviewed: 3 results,  Acknowledgement Compliant: 3 results,  Open Access: 1 results) Presentation (2 results)

  • [Journal Article] Ric-8A-mediated stabilization of the trimeric G protein subunit Gαi is inhibited by pertussis toxin-catalyzed ADP-ribosylation2017

    • Author(s)
      Kanako Chishiki, Sachiko Kamakura, Junya Hayase, Satoru Yuzawa, Hideki Sumimoto
    • Journal Title

      Biochemical and Biophysical Research Communications

      Volume: 483 Issue: 3 Pages: 941-945

    • DOI

      10.1016/j.bbrc.2017.01.036

    • Related Report
      2016 Annual Research Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] Structural basis of cofactor-mediated stabilization and substrate recognition of the α-tubulin acetyltransferase αTAT12015

    • Author(s)
      Yuzawa S, Kamakura S, Hayase J, Sumimoto H
    • Journal Title

      Biochem J.

      Volume: 467 Issue: 2 Pages: 103-113

    • DOI

      10.1107/s2053230x14028143

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Open Access / Acknowledgement Compliant
  • [Journal Article] Structural basis of cofactor-mediated stabilization and substrate recognition of the α-tubulin acetyltransferase αTAT12015

    • Author(s)
      Satoru Yuzawa, Sachiko Kamakura, Junya Hayase and Hideki Sumimoto
    • Journal Title

      Biochemical Journal

      Volume: 467 Issue: 1 Pages: 103-113

    • DOI

      10.1042/bj20141193

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Presentation] アダプタータンパク質LGNのTPRドメインによるスキャフォールドタンパク質Frmpd4/Preso1認識の構造基盤2015

    • Author(s)
      髙栁宏樹,湯澤聡,住本英樹
    • Organizer
      第38回分子生物学会年会・第88回生化学会大会合同大会BMB2015
    • Place of Presentation
      神戸市
    • Year and Date
      2015-12-01
    • Related Report
      2015 Research-status Report
  • [Presentation] α-チューブリンアセチル化酵素αTAT1のコファクターによる安定化の構造基盤2015

    • Author(s)
      湯澤聡,鎌倉幸子,早瀬純也,住本英樹
    • Organizer
      第15回日本蛋白質科学会年会
    • Place of Presentation
      徳島市
    • Year and Date
      2015-06-24
    • Related Report
      2015 Research-status Report

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Published: 2014-04-04   Modified: 2018-03-22  

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