| Project/Area Number |
16K15094
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Kwansei Gakuin University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
HAYASHI Aki 関西学院大学, 理工学部, 助教 (80399534)
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 染色体 / テロメア / 分裂酵母 / タンパク質翻訳後修飾 / SUMO / Rif1 / SUMO翻訳後修飾 / ゲノム |
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| Outline of Final Research Achievements |
Telomeres protect the DNA ends of linear eukaryotic chromosomes from degradation and fusion, as well as ensure complete replication of the DNA terminal through recruitment of telomerase. The regulation of telomerase is a critical area in telomere research in mammals and fission yeast. SUMOylation is known involving in the negative regulation of telomere extension by telomerase. We identified a novel safeguard system to maintain the telomere length. We found that SUMOylation and Rif1 function in a coordinated manner for this safeguard system. Rif1 is a conserved protein that regulates telomere length, replication timing, and repair of double-stranded DNA breaks. Protein phosphatase 1 (PP1) that interacts with Rif1 is known as a key factor for some of Rif1 functions. Furthermore, we have shown the requirement of the PP1 domain of Rif1 for this safeguard system, suggesting that the involvement of dephosphorylation of unknown target protein by Rif1.
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