Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase
AUTOR(ES)
Shimizu, Yuichiro
FONTE
Oxford University Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=140069Documentos Relacionados
- The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein
- Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein
- p53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene
- HPV E6 protein interacts physically and functionally with the cellular telomerase complex
- Xeroderma Pigmentosum Group A Protein Loads as a Separate Factor onto DNA Lesions