Mechanisms for the maintenance of genome stability that involves proteins for the initiation of DNA replication.
| Project/Area Number |
24590089
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Toho University (2014)
Teikyo Heisei University (2012-2013) |
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Principal Investigator |
TADA Shusuke 東邦大学, 薬学部, 教授 (00216970)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | DNA複製 / ゲノム安定性 / RECQL4 / CDT1 / ゲノム安定性維持 / DNA修復 / RecQL4 / Cdc6 / Cdt1 |
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| Outline of Final Research Achievements |
There is increased risk of damage on genetic information when DNA is replicated for cellular proliferation. The aim of the research project is to elucidate the relationship between the proyeins for DNA replication initiation and maintenance of genome stability. From this study, it is suggested that RECQL4, which functions in the initiation of DNA replication and genome stability, possess a functional domain that prevent an essential role of RECQL4 for cellular survival when it is expressed alone. For CDT1, an essential protein for the first step of the initiation of DNA replication (‘licensing’), we have so far proposed that CDT1 suppresses nascent strand elongation of DNA replication. In this study, we further demonstrated that N-terminal 254 amino acids domain of CDT1 is not concerned with this function. Moreover, CDT1 C-terminal domains appeared to be partially related to this function of CDT1.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain.2012
Author(s)
Nomura, H., Yoshimura, A., Edo, T., Kanno, S.I., Tada, S., Seki, M., Yasui, A., and Enomoto, T.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 417
Issue: 4
Pages: 1145-1150
DOI
Related Report
Peer Reviewed
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