Identification of a damaged-DNA binding domain of the XPA protein

被引:99
作者
Kuraoka, I
Morita, EH
Saijo, M
Matsuda, T
Morikawa, K
Shirakawa, M
Tanaka, K
机构
[1] OSAKA UNIV,INST MOLEC & CELLULAR BIOL,SUITA,OSAKA 565,JAPAN
[2] PROT ENGN RES INST,SUITA,OSAKA 565,JAPAN
[3] OSAKA UNIV,INST PROT RES,SUITA,OSAKA 565,JAPAN
来源
MUTATION RESEARCH-DNA REPAIR | 1996年 / 362卷 / 01期
关键词
Xeroderma pigmentosum; DNA-binding; zinc finger motif;
D O I
10.1016/0921-8777(95)00038-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The XPA (xeroderma pigmentosum group A) protein is a zinc metalloprotein consisting of 273 amino acids which binds preferentially to UV- or chemical carcinogen-damaged DNA, suggesting that it is involved in the recognition of several types of DNA damage during nucleotide excision repair processes. Here we identify a DNA binding domain of the XPA protein, The region of the XPA protein responsible for preferential binding to DNA damaged by UV or cis-diammine-dichloroplatinum(II) (cisplatin) is contained within a truncated derivative of the XPA protein, MF122, consisting of 122 amino acids and containing a C-4 type zinc finger motif, CD (circular dichroism) measurements of the MF122 protein showed that it has a helix-rich secondary structure, suggesting that it is a discretely folded, functional mini-domain. The MF122 protein should be useful for structural investigation of the XPA protein and of its interaction with damaged DNA.
引用
收藏
页码:87 / 95
页数:9
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