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本文引用的文献

1
Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain.嗜热栖热菌MCM蛋白N端结构域的结构分析
Nucleic Acids Res. 2008 Jun;36(10):3235-43. doi: 10.1093/nar/gkn183. Epub 2008 Apr 16.
2
The MCM complex: (just) a replicative helicase?MCM复合物：仅仅是一种复制解旋酶吗？
Biochem Soc Trans. 2008 Feb;36(Pt 1):136-40. doi: 10.1042/BST0360136.
3
Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein.DNA结合与解旋酶活性的偶联由MCM蛋白中的一个保守环介导。
Nucleic Acids Res. 2008 Mar;36(4):1309-20. doi: 10.1093/nar/gkm1160. Epub 2008 Jan 9.
4
ATPase site architecture and helicase mechanism of an archaeal MCM.古菌MCM的ATP酶位点结构与解旋酶机制
Mol Cell. 2007 Oct 26;28(2):304-14. doi: 10.1016/j.molcel.2007.08.013.
5
Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.独特的静态和动态相互作用控制AAA+蛋白酶中的ATP酶-肽酶通讯。
Mol Cell. 2007 Jul 6;27(1):41-52. doi: 10.1016/j.molcel.2007.05.024.
6
Archaeal MCM has separable processivity, substrate choice and helicase domains.古菌MCM具有可分离的持续合成能力、底物选择能力和解旋酶结构域。
Nucleic Acids Res. 2007;35(3):988-98. doi: 10.1093/nar/gkl1117. Epub 2007 Jan 26.
7
Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity.嗜热自养甲烷杆菌MCM解旋酶活性的结构基础
Nucleic Acids Res. 2006;34(20):5829-38. doi: 10.1093/nar/gkl708. Epub 2006 Oct 24.
8
Mechanism of DNA translocation in a replicative hexameric helicase.复制性六聚体解旋酶中DNA易位的机制。
Nature. 2006 Jul 20;442(7100):270-5. doi: 10.1038/nature04943.
9
DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase.噬菌体T7 DNA解旋酶中DNA诱导的从独立dTTP水解到顺序dTTP水解的转变
Mol Cell. 2006 Jan 20;21(2):165-74. doi: 10.1016/j.molcel.2005.11.027.
10
Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.重建的AAA+马达揭示了由三磷酸腺苷驱动的机器的工作原理。
Nature. 2005 Oct 20;437(7062):1115-20. doi: 10.1038/nature04031.

由MCM解旋酶中一个保守环介导的亚基间变构通讯。

Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase.

作者信息

Barry Elizabeth R, Lovett Janet E, Costa Alessandro, Lea Susan M, Bell Stephen D

机构信息

MRC Cancer Cell Unit, Hutchison MRC Centre, Hills Road, Cambridge CB2 0XZ, United Kingdom.

出版信息

Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1051-6. doi: 10.1073/pnas.0809192106. Epub 2009 Jan 21.

DOI:10.1073/pnas.0809192106
PMID:19164574
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2633543/
Abstract

The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.

摘要

微小染色体维持（MCM）解旋酶被认为是古细菌和真核生物中的复制性解旋酶。古细菌的同型多聚体MCM具有两层结构。一层包含蛋白质的AAA+马达结构域，这些是最小的功能性解旋酶结构域。第二层由N端结构域形成。这些结构域对于MCM解旋酶活性并非必需，但起到增强解旋酶持续合成能力的作用。我们发现一个保守环促进了持续合成能力层与马达层之间的通讯。有趣的是，这种变构似乎是由MCM环中各个原体之间而非原体内部的相互作用介导的。