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首页> 外文期刊>Journal of Molecular Biology >Switching catalytic activity in the XerCD site-specific recombination machine
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Switching catalytic activity in the XerCD site-specific recombination machine

机译：在XerCD定点重组机器中转换催化活性

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摘要

The tyrosine family site-specific recombinases, XerCD, function in the conversion of circular dimer replicons to monomers. In the recombining complex that contains two synapsed recombination sites and two molecules each of XerC and XerD, the DNA strand-exchange reactions are separated in time and space. XerC initiates recombination to form a Holliday junction intermediate, which undergoes a conformational change to provide a substrate for strand exchange by XerD. XerCD are two-domain proteins, whose C-terminal domains contain all of the catalytic residues. We show that XerC or XerD variants lacking their N-terminal domains are active in recombination when combined with their wild-type partner. Nevertheless, the normal pattern of catalysis is dramatically altered; strand exchange by the recombinase variant is stimulated, while that by the wild-type partner recombinase is impaired. The primary determinants for the mutant phenotype reside in the region of alpha -helix B of XerD. We propose that altered interactions within the recombining heterotetramer lead to changes in the relative concentrations of the two alternative Holliday junction substrates that are recombined by XerC or XerD, respectively.
机译：酪氨酸家族位点特异性重组酶XerCD在环状二聚体复制子向单体的转化中起作用。在包含两个突触重组位点和两个分子XerC和XerD的重组复合物中，DNA链交换反应在时间和空间上是分开的。 XerC启动重组以形成霍利迪连接中间体，该中间体经历构象变化，从而为XerD交换链提供底物。 XerCD是两个结构域的蛋白质，其C端结构域包含所有催化残基。我们显示缺少其N末端域的XerC或XerD变体与它们的野生型伴侣结合时在重组中具有活性。然而，催化的正常模式已大大改变。重组酶变体刺激链交换，而野生型伴侣重组酶则损害链交换。突变表型的主要决定因素位于XerD的α-螺旋B区域。我们提出，重组异四聚体中相互作用的改变会导致分别由XerC或XerD重组的两个替代霍利迪结底物的相对浓度发生变化。

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