Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function.
Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function.
复制标题
古菌 MCM 蛋白作为真核 Mcm2-7 解旋酶的类似物，揭示结构和功能的基本特征。
DOI：
10.1155/2015/305497
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Enemark,EricJ
中科院分区：
文献类型：
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作者：
Miller,JustinM;Enemark,EricJ
在真核生物中，复制解旋酶是由 Mcm2-7 六聚环、Cdc45 和四聚 GINS 复合物组成的大型多亚基 CMG 复合物。 Mcm2-7 环由六种不同的相关蛋白质组装而成，并形成该复合物的核心。在古细菌中，同源的 MCM 六聚环充当复制叉处的复制解旋酶。古细菌 MCM 蛋白形成热稳定的同源六聚体，有利于它们用作真核 Mcm2-7 解旋酶的模型。在这里，我们回顾了古菌 MCM 解旋酶的结构和功能，以及古菌发现与真核 Mcm2-7 环的关系。
In eukaryotes, the replicative helicase is the large multisubunit CMG complex consisting of the Mcm2–7 hexameric ring, Cdc45, and the tetrameric GINS complex. The Mcm2–7 ring assembles from six different, related proteins and forms the core of this complex. In archaea, a homologous MCM hexameric ring functions as the replicative helicase at the replication fork. Archaeal MCM proteins form thermostable homohexamers, facilitating their use as models of the eukaryotic Mcm2–7 helicase. Here we review archaeal MCM helicase structure and function and how the archaeal findings relate to the eukaryotic Mcm2–7 ring.