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Structure of the EndoMS-DNA Complex as Mismatch Restriction Endonuclease

机译：EndoMS-DNA复合物的结构，作为错配限制核酸内切酶

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摘要

Archaeal NucS nuclease was thought to degrade the single-stranded region of branched DNA, which contains flapped and splayed DNA. However, recent findings indicated that EndoMS, the orthologous enzyme of NucS, specifically cleaves double-stranded DNA (dsDNA) containing mismatched bases. In this study, we determined the structure of the EndoMS-DNA complex. The complex structure of the EndoMS dimer with dsDNA unexpectedly revealed that the mismatched bases were flipped out into binding sites, and the overall architecture most resembled that of restriction enzymes. The structure of the apo form was similar to the reported structure of Pyrococcus abyssi NucS, indicating that movement of the C-terminal domain from the resting state was required for activity. In addition, a model of the EndoMS-PCNA-DNA complex was preliminarily verified with electron microscopy. The structures strongly support the idea that EndoMS acts in a mismatch repair pathway.
机译：人们认为古细菌NucS核酸酶可降解分支DNA的单链区域，其中包含拍打和张开的DNA。但是，最近的发现表明，NucS的直系同源酶EndoMS特异地裂解了碱基错配的双链DNA（dsDNA）。在这项研究中，我们确定了EndoMS-DNA复合物的结构。 EndoMS二聚体与dsDNA的复杂结构出乎意料地表明，错配的碱基被翻转到结合位点，总体结构与限制酶最为相似。载脂蛋白形式的结构类似于所报道的深渊热球菌NucS的结构，表明C末端结构域从静止状态的移动是活性所必需的。另外，通过电子显微镜初步验证了EndoMS-PCNA-DNA复合物的模型。这些结构强烈支持EndoMS在错配修复途径中起作用的想法。

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