THE DNA-BINDING PROPERTIES OF THE MUTL PROTEIN ISOLATED FROM ESCHERICHIA-COLI

被引：54

作者：

BENDE, SM ^{[1
]}

GRAFSTROM, RH ^{[1
]}

机构：

[1] THOMAS JEFFERSON UNIV,JEFFERSON MED COLL,DEPT MICROBIOL & IMMUNOL,PHILADELPHIA,PA 19107

来源：

NUCLEIC ACIDS RESEARCH | 1991年 / 19卷 / 07期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1093/nar/19.7.1549

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mutL gene of Escherichia coli, which is involved in the repair of mispaired and unpaired nucleotides in DNA, has been independently cloned and the gene product purified. In addition to restoring methyl-directed DNA repair in extracts prepared from mutL strains, the purified MutL protein binds to both double and single stranded DNA. The affinity constant of MutL for unmethylated single stranded DNA was twice that of its affinity constant for methylated single stranded DNA and methylated or unmethylated double stranded DNA. The binding of MutL to double stranded DNA was not affected by the pattern of DNA methylation or the presence of a MutHLS-repairable lesion.

引用

页码：1549 / 1555

页数：7

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