Biochemical and dynamic structural analysis of translesion DNA polymerase

2014 Fiscal Year Final Research Report

• Project/Area Number: 24510066
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Risk sciences of radiation/Chemicals
• Research Institution: Nagasaki University (2014); Kumamoto University (2013); Chiba University (2012)
• Principal Investigator: KARATA Kiyonobu 長崎大学, 原爆後障害医療研究所, 産学官連携研究員 (90345017)
• Co-Investigator(Renkei-kenkyūsha): OGURA Teru 熊本大学, 発生医学研究所, 教授 (00158825)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: DNA複製 / 損傷乗り越え

Outline of Final Research Achievements

DNA polymerase V is responsible for most mutations that arise from DNA damages in E. coli. We found that Pol V can incorporate ribonucleotide as well as deoxyribonucleotide and proposed a new model referred to as “ribonucleotide excision repair (RER)”. In the model, a part of Pol V-synthesized strand is resynthesized by error-free DNA polymerase utilizing ribonucleotide-deoxyribonucleotide hybrid region and it leads to a reduction of mutation frequency. We also found that RecA bound to UmuC, Pol V’s catalytic subunit, in 2 different regions. One was for active Pol V, and the other was for inactive Pol V.

Free Research Field

分子生物学