Elucidation of a novel DNA repair system from extremophiles and application to exploit of an available host.
| Project/Area Number |
23880022
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied microbiology
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| Research Institution | Kyushu University |
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Principal Investigator |
MORITA Rihito 九州大学, 大学院・農学研究院, 学術研究員 (10613268)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | アーキア / 多機能酵素 / マルチドメイン / 極限環境微生物 / DNA 修復 / アルキル化傷害 / DNA修復系 / 有用宿主 |
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| Research Abstract |
A novel proteins likely involved in multiple DNA repair systems were found in extremophiles. These proteins are comprised of two domains, an alkylated lesion repair protein-like domain in N-terminus and an Endonuclease V (EndoV)-like domain, deamination repair protein, in C-terminus. However, the pathways which is involved in these novel proteins are completely unknown. Since the most of extremophiles are unculturable and their genome sequences are unclear, the novel DNA repair systems potentially act in important pathway from extremophiles. From my prediction, it is important as applications and basic science to elucidate the functions of these novel proteins, AGT-EndoV and ATL-EndoV. I tried to elucidate the function in this project.
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Report
(3 results)
Research Products
(10 results)
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[Journal Article] Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-πinteractions.2012
Author(s)
Oliver J. Wilkinson, Vitaly Latypov, Julie L. Tubbsc, Christopher L. Millington, Rihito Morita, Hannah Blackburn, Andrew Marriott, Gail McGown, Mary Thorncroft, Amanda J. Watson, Bernard A. Connolly, Jane A. Grasby, Ryoji Masui, Christopher A. Huntera, Jo
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Journal Title
Proceedings of the National Academy of Sciences ofthe United States of America
Volume: vol 109
Pages: 18755-18760
Related Report
Peer Reviewed
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