Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.

Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.
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与霍利迪连接解离酶 Hjc 相互作用并促进分支迁移的新型 ATP 酶的结构和功能

DOI:
10.1016/j.jmb.2017.02.016
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发表时间:
2017-04-07
影响因子:
5.6
通讯作者:
Fan L
Fan L
中科院分区:
生物学2区
文献类型:
--
作者:
Zhai B;DuPrez K;Doukov TI;Li H;Huang M;Shang G;Ni J;Gu L;Shen Y;Fan L

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Holliday连接(HJ)是DNA重组的标志性中间体,必须通过溶解(对于双HJ)或拆分来处理,以确保基因组的稳定性。虽然HJ分解酶在生命的所有领域都已被发现,但在原核生物和真核生物中寻找促进HJ迁移的蛋白质的努力由来已久。在这里,我们报道了一个新的ATPase,Sulfolobus islandicus PILT N-末端结构域含ATPase(SisPINA),它是由解析酶HJC编码基因编码的。PINA在古生菌中是保守的,对岛链霉菌的生存至关重要。纯化的SisPINA在结晶态和溶液中形成六聚体环,类似于革兰氏阴性细菌中的HJ迁移解旋酶RuvB。结构分析表明,ATP结合和水解导致SisPINA的构象变化,从而驱动分支迁移。进一步的研究表明,SisPINA与SisHjc相互作用,并协调HJ的迁移和切割。
Holliday junction (HJ) is a hallmark intermediate in DNA recombination and must be processed by dissolution (for double HJ) or resolution to ensure genome stability. Although HJ resolvases have been identified in all domains of life, there is a long-standing effort to search in prokaryotes and eukarya for proteins promoting HJ migration. Here, we report the structural and functional characterization of a novel ATPase, Sulfolobus islandicus PilT N-terminal-domain-containing ATPase (SisPINA), encoded by the gene adjacent to the resolvase Hjc coding gene. PINA is conserved in archaea and vital for S. islandicus viability. Purified SisPINA forms hexameric rings in the crystalline state and in solution, similar to the HJ migration helicase RuvB in Gram-negative bacteria. Structural analysis suggests that ATP binding and hydrolysis cause conformational changes in SisPINA to drive branch migration. Further studies reveal that SisPINA interacts with SisHjc and coordinates HJ migration and cleavage.
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