古细菌MCM蛋白作为真核Mcm2-7解旋酶的类似物揭示其结构和功能的基本特征

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS ACS Applied Bio Materials Pub Date : 2015-10-11 DOI:10.1155/2015/305497
Justin M. Miller, E. J. Enemark
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引用次数: 21

摘要

在真核生物中,复制解旋酶是由Mcm2-7六聚体环、Cdc45和四聚体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合而成,形成了这个复合物的核心。在古细菌中,同源的MCM六聚体环在复制叉上起着复制解旋酶的作用。古细菌MCM蛋白形成耐热的同六聚体,便于它们作为真核Mcm2-7解旋酶的模型。本文综述了古细菌MCM解旋酶的结构和功能,以及这些发现与真核生物Mcm2-7环的关系。
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Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2–7 Helicase to Reveal Essential Features of Structure and Function
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.
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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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