The beta protein of phage λ binds preferentially to an intermediate in DNA renaturation
The beta protein of phage λ binds preferentially to an intermediate in DNA renaturation
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DOI：
10.1006/jmbi.1997.1573
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发表时间：
1998-03-06
影响因子：
5.6
通讯作者：
Radding, CM
中科院分区：
文献类型：
--
作者：
Karakousis, G;Ye, N;Radding, CM
λ噬菌体编码两种重组蛋白，这两种重组蛋白是recA（-）宿主菌株中同源重组所需的。在这两种重组蛋白中，一种是外切核酸酶，其作用于双链DNA产生3'单链末端;另一种称为β蛋白，是DNA结合蛋白，其促进互补单链的复性。λ噬菌体的酶提供了一个模型，用于理解称为“单链退火”的重组途径。对β蛋白与DNA结合的进一步研究揭示了一种新的复性机制。如前所述，β蛋白直接与单链DNA结合，但不与双链DNA结合。然而，在这里报道的实验中，我们观察到β蛋白更强烈地结合到β本身催化的复性反应中的假定中间体，从而保护所有复性的双链体83-mer寡核苷酸免受核酸酶消化。(C)出版社：Academic Press Limited。
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.