Analysis of Translesion synthesis (TLS) mechanism by novel assay method
| Project/Area Number |
16K12598
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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 |
Risk sciences of radiation and chemicals
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| Research Institution | Tokyo Metropolitan University |
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Principal Investigator |
Hirota Kouji 首都大学東京, 理工学研究科, 教授 (00342840)
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| Research Collaborator |
Julian Sale ケンブリッジ大, 教授
Doherty Aidan サセックス大, 教授
Branzei Dana IFOM研究所, 教授
Scott Keeney スローンケタリング癌研究所, 教授
Hoffman Charles S. ボストン大, 教授
Pommier Yves NIH, 教授
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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: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | DNA損傷 / 損傷乗り越え / TLSポリメラーゼ / 変異 / 紫外線 / CPD / ポリメラーゼ / 複製 |
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| Outline of Final Research Achievements |
Translesion DNA synthesis (TLS) is pivotal for releasing replication arrest at DNA damage on the template strand. TLS polymerases are involved in this bypass replication across damaged template. However, the mechanism to select a polymerase to carry out TLS across some specific damage has not been elucidated. For the bypass of UV induced T-T dimer damage, Polymerase-η can replicate in error free manner, while other TLS polymerases induce replication erorrs during TLS and thereby induce mutations. In this study, we employed novel TLS assay using artifical damaged oligo DNAs and revealed selectivity of TLS polymerase to the kind of DNA damage.
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Report
(3 results)
Research Products
(58 results)
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[Journal Article] ALC1/CHD1L, a chromatin-remodeling enzyme, is required for efficient base excision repair.2017
Author(s)
Tsuda M, Cho K, Ooka M, Shimizu N, Watanabe R, Yasui A, Nakazawa Y, Ogi T, Harada H, Agama K, Nakamura J, Asada R, Fujiike H, Sakuma T, Yamamoto T, Murai J, Hiraoka M, Koike K, Pommier Y, Takeda S, Hirota K.
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Journal Title
PLos One
Volume: 12
Issue: 11
Pages: e0188320-e0188320
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] The dominant role of proofreading exonuclease activity of replicative polymerase ε in cellular tolerance to cytarabine (Ara-C).2017
Author(s)
Tsuda M, Terada K, Ooka M, Kobayashi K, Sasanuma H, Fujisawa R, Tsurimoto T, Yamamoto J, Iwai S, Kadoda K, Akagawa R, Huang SN, Pommier Y, Sale JE, Takeda S, Hirota K.
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Journal Title
Oncotarget
Volume: in press
Issue: 20
Pages: 33457-33474
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] The Dominant Role of Proofreading Exonuclease Activity of Replicative Polymerase ε in Cellular Tolerance Contributes to Cellular Tolerance of Cytarabine (Ara-C)2017
Author(s)
Masataka Tsuda, Kazuhiro Terada, Masato Ooka, Koji Kobayashi, Hiroyuki Sasanuma, Ryo Fujisawa, Toshiki Tsurimoto, Junpei Yamamoto, Shigenori Iwai, Kei Kadoda, Remi Akagawa, Shar-yin Naomi Huang, Yves Pommier, Julian E. Sale, Shunichi Takeda, and Kouji Hirota
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Journal Title
Oncotarget
Volume: in press
Related Report
Peer Reviewed / Int'l Joint Research
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[Journal Article] In vivo evidence for translesion synthesis by the replicative DNA polymerase δ.2016
Author(s)
Hirota K, Tsuda M, Mohiuddin, Tsurimoto T, Cohen IS, Livneh Z, Kobayashi K, Narita T, Nishihara K, Murai J, Iwai S, Guilbaud G, Sale JE, Takeda S.
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Journal Title
Nucleic Acids Res
Volume: 44(15)
Pages: 7242-50
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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