真核病毒中的细菌型DNA霍利迪连接体解离酶。
Bacterial-type DNA holliday junction resolvases in eukaryotic viruses.
作者信息
Garcia A D, Aravind L, Koonin E V, Moss B
机构信息
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, and National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20892, USA.
出版信息
Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8926-31. doi: 10.1073/pnas.150238697.
Abstract
Homologous DNA recombination promotes genetic diversity and the maintenance of genome integrity, yet no enzymes with specificity for the Holliday junction (HJ)-a key DNA recombination intermediate-have been purified and characterized from metazoa or their viruses. Here we identify critical structural elements of RuvC, a bacterial HJ resolvase, in uncharacterized open reading frames from poxviruses and an iridovirus. The putative vaccinia virus resolvase was expressed as a recombinant protein, affinity purified, and shown to specifically bind and cleave a synthetic HJ to yield nicked duplex molecules. Mutation of either of two conserved acidic amino acids abrogated the catalytic activity of the A22R protein without affecting HJ binding. The presence of bacterial-type enzymes in metazoan viruses raises evolutionary questions.
摘要
同源DNA重组促进了遗传多样性和基因组完整性的维持，但尚未从后生动物或其病毒中纯化和鉴定出对霍利迪连接体（HJ）（一种关键的DNA重组中间体）具有特异性的酶。在这里，我们在痘病毒和一种虹彩病毒的未表征开放阅读框中鉴定出细菌HJ解旋酶RuvC的关键结构元件。假定的痘苗病毒解旋酶被表达为重组蛋白，经亲和纯化后，显示出特异性结合并切割合成的HJ，产生带切口的双链分子。两个保守酸性氨基酸中的任何一个发生突变都会消除A22R蛋白的催化活性，而不影响HJ结合。后生动物病毒中存在细菌型酶引发了进化问题。
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