The investigation of the feedback regulation for interplay between DNA damage detection and repair
Project/Area Number |
24687023
|
Research Category |
Grant-in-Aid for Young Scientists (A)
|
Allocation Type | Partial Multi-year Fund |
Research Field |
Molecular biology
|
Research Institution | Kyoto University |
Principal Investigator |
FURUYA Kanji 京都大学, 放射線生物研究センター, 講師 (90455204)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥27,560,000 (Direct Cost: ¥21,200,000、Indirect Cost: ¥6,360,000)
Fiscal Year 2014: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
Fiscal Year 2013: ¥8,970,000 (Direct Cost: ¥6,900,000、Indirect Cost: ¥2,070,000)
Fiscal Year 2012: ¥11,700,000 (Direct Cost: ¥9,000,000、Indirect Cost: ¥2,700,000)
|
Keywords | DNA損傷 / チェックポイント / DNA修復 / 放射線 / リン酸化 / ダイナミクス / タンパク質分解 / ATP分解酵素 / 分子生物 / キナーゼ / Rad9 |
Outline of Final Research Achievements |
Ionizing irradiation and ultraviolets could alter genetic information by damaging genomic DNA. The damaged DNA should be detected and then repaired. For accurate and quick restoration of DNA information, DNA damage detection system and repair system must cooperate, however the underlying mechanism of that is still largely unknown. In this study, we focus on one of the checkpoint protein Rad9, and analyzed in order to understand the positive and negative feedback system that regulate Rad9 behavior from activation to inactivation, by phosphorylation. First, we constructed the in vitro reconstitution system to investigate the interaction between Rad9 complex and its loader complex to DNA damage site, Rad17 complex. The ATP dependent interaction is observed and suggested that ATP dependent conformational change govern the regulation. Furthermore we identified Plk1 as a negative regulator that phsphorylate human Rad9 orthologue.
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Report
(4 results)
Research Products
(21 results)