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首页> 外文期刊>Nucleic Acids Research >Physical and functional interactions between Escherichia coli MutL and the Vsr repair endonuclease.
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Physical and functional interactions between Escherichia coli MutL and the Vsr repair endonuclease.

机译：大肠杆菌MutL和Vsr修复核酸内切酶之间的物理和功能相互作用。

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摘要

DNA mismatch repair (MMR) and very-short patch (VSP) repair are two pathways involved in the repair of T:G mismatches. To learn about competition and cooperation between these two repair pathways, we analyzed the physical and functional interaction between MutL and Vsr using biophysical and biochemical methods. Analytical ultracentrifugation reveals a nucleotide-dependent interaction between Vsr and the N-terminal domain of MutL. Using chemical crosslinking, we mapped the interaction site of MutL for Vsr to a region between the N-terminal domains similar to that described before for the interaction between MutL and the strand discrimination endonuclease MutH of the MMR system. Competition between MutH and Vsr for binding to MutL resulted in inhibition of the mismatch-provoked MutS- and MutL-dependent activation of MutH, which explains the mutagenic effect of Vsr overexpression. Cooperation between MMR and VSP repair was demonstrated by the stimulation of the Vsr endonuclease in a MutS-, MutL- and ATP-hydrolysis-dependent manner, in agreement with the enhancement of VSP repair by MutS and MutL in vivo. These data suggest a mobile MutS-MutL complex in MMR signalling, that leaves the DNA mismatch prior to, or at the time of, activation of downstream effector molecules such as Vsr or MutH.
机译：DNA错配修复（MMR）和超短补丁（VSP）修复是T：G错配修复的两个途径。为了了解这两种修复途径之间的竞争与合作，我们使用生物物理和生化方法分析了MutL和Vsr之间的物理和功能相互作用。分析性超速离心揭示了Vsr和MutL N末端结构域之间的核苷酸依赖性相互作用。使用化学交联，我们将针对Vsr的MutL的相互作用位点映射到N末端结构域之间的区域，类似于之前针对MutL和MMR系统的链区分核酸内切酶MutH之间的相互作用所描述的区域。 MutH和Vsr之间竞争与MutL的竞争导致抑制不匹配引起的MutH和MutL依赖的MutH激活，这解释了Vsr过表达的诱变作用。 MMR和VSP修复之间的合作通过以MutS，MutL和ATP水解依赖性方式刺激Vsr核酸内切酶来证明，这与MutS和MutL在体内增强VSP修复相一致。这些数据表明在MMR信号中存在一个可移动的MutS-MutL复合物，在激活下游效应分子（如Vsr或MutH）之前或之时，DNA错配。

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