Functional analyses of translesion synthesis DNA polymerase Poleta based on its structural features

2017 Fiscal Year Final Research Report

• Project/Area Number: 26340028
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Risk sciences of radiation and chemicals
• Research Institution: Kobe University (2016-2017); Gakushuin University (2014-2015)
• Principal Investigator: YOKOI MASAYUKI 神戸大学, バイオシグナル総合研究センター, 准教授 (00322701)
• Project Period (FY): 2014-04-01 – 2018-03-31
• Keywords: 損傷乗り越え合成

Outline of Final Research Achievements

Human Poleta is a major translesion synthesis polymerase involved in DNA damage tolerance against UV- or cisplatin-induced DNA lesions. To elucidate its physiological function and regulatory mechanism in cellular DNA damage tolerance, I focused on unique structural features of human Poleta identified from the comparison of its crystal structure against other eukaryotic TLS polymerases. As a result, unique amino acid sequences or amino acid residues of human Poleta were deleted or substituted by other amino acid to investigate their role. Biochemical and cellular analyses using these mutant proteins revealed that some of them were important for the translesion synthesis activity or regulation of human Poleta. It was notable, in this research, that several novel proteins and chemical compounds were identified to interact with or regulate human Poleta. These findings will open new phase of research on DNA damage tolerance associated with human Poleta.

Free Research Field

分子生物学