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Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase
Author(s) -
Shimizu Yuichiro,
Iwai Shigenori,
Hanaoka Fumio,
Sugasawa Kaoru
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg016
Subject(s) - xeroderma pigmentosum , biology , dna glycosylase , thymine , dna , dna repair , genetics , nucleotide excision repair , group (periodic table) , microbiology and biotechnology , chemistry , organic chemistry
The XPC–HR23B complex recognizes various helix‐distorting lesions in DNA and initiates global genome nucleotide excision repair. Here we describe a novel functional interaction between XPC–HR23B and thymine DNA glycosylase (TDG), which initiates base excision repair (BER) of G/T mismatches generated by spontaneous deamination of 5‐methylcytosine. XPC–HR23B stimulated TDG activity by promoting the release of TDG from abasic sites that result from the excision of mismatched T bases. In the presence of AP endonuclease (APE), XPC–HR23B had an additive effect on the enzymatic turnover of TDG without significantly inhibiting the subsequent action of APE. Our observations suggest that XPC–HR23B may participate in BER of G/T mismatches, thereby contributing to the suppression of spontaneous mutations that may be one of the contributory factors for the promotion of carcinogenesis in xeroderma pigmentosum genetic complementation group C patients.