A novel GT-mismatch binding protein that recognizes strict DNA sequences with high affinity

被引:2
作者
Takata-Yahiro, M
Fujii, Y
Nodarse, JF
Islam, MR
Oda, S
Zhang, QM
Yonei, S
Nakamura, M
机构
[1] Nagasaki Univ, Inst Trop Med, Dept Host Def Biochem, Nagasaki 8528523, Japan
[2] Kyushu Natl Canc Ctr, Inst Clin Res, Fukuoka 8111395, Japan
[3] Kyoto Univ, Grad Sch Sci, Radiat Biol Lab, Kyoto 6068502, Japan
关键词
GT-mismatch binding protein; DNA repair; deamination; gp91(phox) promoter;
D O I
10.1620/tjem.200.211
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Mismatched or damaged base pairs in DNA are mutagenic and both eukaryotes and prokaryotes have a series of repair systems that decrease a spontaneous mutation rate. All exocyclic amino groups of cytosine(C), adenine(A), and guanine(G) contribute to hydrogen bonds for base pairing. High temperature and oxidative stresses increase the deamination of these bases and methylated C. These deaminated sites would be initially recognized by components of DNA repair system. We discovered a novel G/thymine(T)-mismatch binding protein (nGTBP) that bound, with high affinity, to a minimal 14-mer DNA heteroduplex with a strict 5'-TRTGNB-3' sequence (R for purine, N for any bases, and B for "not A," namely for C, G, or T). This italicized G position mismatched with T could be replaced by hypoxanthine, the deaminated A. The nGTBP, however, barely recognized DNA duplexes individually containing 8-oxo-G, thymine glycol, and 5-methylcytosine. (C) 2003 Tohoku University Medical Pres.
引用
收藏
页码:211 / 229
页数:19
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