Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein.

Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein.
复制标题

DNA结合和解旋酶活性的偶联是由MCM蛋白中的保守环介导的。

DOI:
10.1093/nar/gkm1160
复制
发表时间:
2008-03
影响因子:
14.9
通讯作者:
Kelman, Zvi
Kelman, Zvi
中科院分区:
生物学2区
文献类型:
--
作者:
Sakakibara, Nozomi;Kasiviswanathan, Rajesh;Melamud, Eugene;Han, Mimi;Schwarz, Frederick P.;Kelman, Zvi

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微小染色体维持(MCM)解旋酶是假定的复制解旋酶,被认为在复制期间分离染色体DNA的两条链。在古细菌中,催化活性存在于MCM蛋白的C-末端区域内。在嗜热甲烷杆菌中,蛋白质的N-末端部分被证明参与蛋白质多聚化和与单链和双链DNA的结合。来自许多古细菌物种的MCM同源物在位于分子的N-末端部分的β7和β8之间的环中具有高度保守的预测氨基酸相似性。这种高度的保守性表明了环的功能作用。保守残基的突变分析和生化表征表明,该环参与解旋酶的N-末端部分和C-末端催化结构域之间的通信。由于类似的残基也是保守的真核MCM蛋白,这里提出的数据表明,类似的偶联N-末端和真核酶的催化结构域之间。
Minichromosome maintenance (MCM) helicases are the presumptive replicative helicases, thought to separate the two strands of chromosomal DNA during replication. In archaea, the catalytic activity resides within the C-terminal region of the MCM protein. In Methanothermobacter thermautotrophicus the N-terminal portion of the protein was shown to be involved in protein multimerization and binding to single and double stranded DNA. MCM homologues from many archaeal species have highly conserved predicted amino acid similarity in a loop located between β7 and β8 in the N-terminal part of the molecule. This high degree of conservation suggests a functional role for the loop. Mutational analysis and biochemical characterization of the conserved residues suggest that the loop participates in communication between the N-terminal portion of the helicase and the C-terminal catalytic domain. Since similar residues are also conserved in the eukaryotic MCM proteins, the data presented here suggest a similar coupling between the N-terminal and catalytic domain of the eukaryotic enzyme.
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