Crystallographic analysis of TFII-I related multiple complexes in Translesion DNA synthesis

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K18491
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: University of Shizuoka
• Principal Investigator: Hara Kodai 静岡県立大学, 薬学部, 助教 (80729343)
• Research Collaborator: YU Hongtao 米国テキサス大学, サウスウエスタンメディカルセンター, 教授
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: X線結晶構造解析 / タンパク質複合体 / DNA修復

Outline of Final Research Achievements

TFII-I is a novel factor in translesion DNA synthesis (TLS) field and functions to recruit other TLS proteins such as DNA replication factor PCNA and DNA polymerase zeta on DNA damaged site. TLS is the strange cellular system to inhibit DNA replication arrest and to promote DNA synthesis even so DNA synthesis is error prone, when the damaged DNA occurs in the endogenous genome during the S-phase. TLS pathway also contributes to acquire the resistance for anticancer drug, thus it is attractive target to develop novel drug. Remarkably, recent study implies TFII-I possibly contributes to Williams-Beuren syndrome, a genetic disorder. To understand molecular mechanism of diseases and the anticancer drug resistance, we have determined structures of TFII-I-PCNA and TFII-I-Pol zeta complexes at each 2.3-3.8 and 4.4 angstrom. however our structures didn't involve in any densities of TFII-I, thus it may be required for continuous approach.

Free Research Field

構造生物学