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Nuclear morphology checkpoint: analysis of the nuclear division arrest caused

Research Project

Project/Area Number 25660055
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Applied microbiology
Research InstitutionKyoto University

Principal Investigator

Yoshiharu Inoue  京都大学, (連合)農学研究科(研究院), 准教授 (70203263)

Project Period (FY) 2013-04-01 – 2016-03-31
Project Status Completed (Fiscal Year 2015)
Budget Amount *help
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Keywordsメチルグリオキサール / 酵母 / 核分裂 / ホスファチジルイノシトール3.5-ビスリン酸 / 核形態 / 液胞 / DNA損傷チェックポイント / Saccharomyces cerevisiae / チェックポイントキナーゼ / セキュリン / セパラーゼ / コヒーシン / ホスファチジルイノシトール
Outline of Final Research Achievements

Methylglyoxal (MG) is derived from glycolysis. We found that MG inhibited the nuclear division in yeast. MG treatment changed yeast vacuole to a single enlarged shape, which altered the nuclear morphology to one with a central depression aligned with the mother-bud axis, which we referred to as a “jellybean-like shape” nucleus. We showed that the levels of phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) were increased with MG treatment. PI(3,5)P2 levels did not increase in mutants defective in Fig4 or Vac14 following treatment with MG, and these mutants did not show the MG-induced nuclear division arrest. Atg18, a PI(3,5)P2-binding protein, was enriched on the vacuolar membrane with MG treatment, and the deletion of ATG18 suppressed the inhibitory effect of MG on nuclear division. We showed that MG activated the DNA damage checkpoint. Degradation of cohesin was inhibited in the presence of MG, which indicated that sister chromatid segregation was stalled.

Report

(4 results)
  • 2015 Annual Research Report   Final Research Report ( PDF )
  • 2014 Research-status Report
  • 2013 Research-status Report
  • Research Products

    (4 results)

All 2016 2015 2014

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

  • [Journal Article] Methylglyoxal activates target of rapamycin complex 2―protein kinase C signaling pathway in Saccharomyces cerevisiae.2015

    • Author(s)
      Nomura, W, and Inoue, Y.
    • Journal Title

      Molecular and Cellular Biology

      Volume: 35 Pages: 1269-1280

    • NAID

      120005615637

    • Related Report
      2015 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] Methylglyoxal Activates the Target of Rapamycin Complex 2-Protein Kinase C Signaling Pathway in Saccharomyces cerevisiae.2015

    • Author(s)
      Nomura, W., and Inoue, Y.
    • Journal Title

      Mol. Cell. Biol.

      Volume: 35 Issue: 7 Pages: 1269-1280

    • DOI

      10.1128/mcb.01118-14

    • Related Report
      2014 Research-status Report
    • Peer Reviewed
  • [Presentation] メチルグリオキサールによる酵母DNA損傷チェックポイントの活性化2016

    • Author(s)
      塩尻敦史、野村 亘、井上善晴
    • Organizer
      日本農芸化学会関西支部第493回講演会
    • Place of Presentation
      楽友会館(京都市左京区)
    • Year and Date
      2016-02-06
    • Related Report
      2015 Annual Research Report
  • [Presentation] TORC2-Pkc1シグナル経路のDNA損傷応答への関与2014

    • Author(s)
      野村 亘、河田照雄、井上善晴
    • Organizer
      第47回酵母遺伝学フォーラム
    • Place of Presentation
      東京大学
    • Year and Date
      2014-09-01 – 2014-09-03
    • Related Report
      2014 Research-status Report

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Published: 2014-07-25   Modified: 2019-07-29  

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