The beta protein of phage λ binds preferentially to an intermediate in DNA renaturation

被引:63
作者
Karakousis, G
Ye, N
Li, Z
Chiu, SK
Reddy, G
Radding, CM [1 ]
机构
[1] Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Dept Mol Biophys, New Haven, CT 06510 USA
[3] Yale Univ, Sch Med, Dept Biochem, New Haven, CT 06510 USA
关键词
recombination; beta protein; bacteriophage lambda; DNA renaturation; DNA binding;
D O I
10.1006/jmbi.1997.1573
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
Phage lambda encodes two recombination proteins that are required for homologous recombination in a recA(-) host strain. Of these two recombination proteins, one is an exonuclease whose action on double-stranded DNA produces 3' single-stranded ends; the other, called beta protein, is a DNA binding protein that promotes the renaturation of complementary single strands. The enzymes of phage lambda provide a model for understanding a recombination pathway called "single-strand annealing". Further investigation of the binding of beta protein to DNA has revealed a new mechanism of renaturation. As reported before, beta protein binds directly to single-stranded DNA, but not to double-stranded DNA. However, in the experiments reported here, we observed that beta protein bound more strongly to a presumed intermediate in the renaturation reaction that beta itself catalyzed, and beta thereby protected all of a renatured duplex 83-mer oligonucleotide from nuclease digestion. (C) 1998 Academic Press Limited.
引用
收藏
页码:721 / 731
页数:11
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