PCNA activates the Holliday junction endonuclease Hjc
PCNA activates the Holliday junction endonuclease Hjc
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DOI：
10.1016/j.jmb.2006.09.011
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发表时间：
2006-12-01
影响因子：
5.6
通讯作者：
White, Malcolm F.
中科院分区：
文献类型：
--
作者：
Dorazi, Robert;Parker, Joanne L.;White, Malcolm F.
分解酶Hjc以高度的结构特异性切割霍利迪连接，在所有古细菌中是保守的。像大肠杆菌中的RuvC一样，Hjc在同源重组和双链断裂修复的相关过程中发挥作用。在细菌中，RuvAB复合物结合霍利迪连接并催化ATP依赖性分支迁移，但古细菌和真核生物中的等效蛋白质尚不清楚。在这里，我们表明，从硫磺硫化叶菌Hjc形成一个物理相互作用的滑动钳PCNA通过C-末端PCNA相互作用肽（PIP）基序Hjc。PCNA在体外刺激Hjc的Holliday连接切割活性，而PIP基序的缺失消除了这种作用。这是第一次报告之间的功能相互作用的滑动钳和连接解析酶，并提出了可能性，PCNA可以招募各种不同的蛋白质在体内霍利迪路口。(c)2006爱思唯尔有限公司保留所有权利。
The resolving enzyme Hjc, which cleaves Holliday junctions with a high degree of structural specificity, is conserved in all archaea. Like RuvC in Escherichia coli, Hjc functions in the related processes of homologous recombination and double-strand break repair. In bacteria, the RuvAB complex binds Holliday junctions and catalyses ATP-dependent branch migration, but the equivalent proteins in archaea and eukarya are unknown. Here, we demonstrate that Hjc from Sulfolobus solfataricus forms a physical interaction with the sliding clamp PCNA via a C-terminal PCNA-interacting peptide (PIP) motif in Hjc. PCNA stimulates the Holliday junction cleavage activity of Hjc in vitro, and deletion of the PIP motif abrogates this effect. This is the first report of a functional interaction between a sliding clamp and a junction-resolving enzyme, and raises the possibility that PCNA could recruit a variety of different proteins to act on Holliday junctions in vivo. (c) 2006 Elsevier Ltd. All rights reserved.