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
中科院分区:
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
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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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
3
作者:
Das, Uddipan;Pogenberg, Vivian;Srinivasan, Alagiri
通讯作者:
Srinivasan, Alagiri
影响因子:
4.8
作者:
Fujikane, R;Komori, K;Ishino, Y
通讯作者:
Ishino, Y
影响因子:
14.9
作者:
Daiyasu, H;Komori, K;Toh, H
通讯作者:
Toh, H
影响因子:
2.1
作者:
Fujikane, R;Shinagawa, H;Ishino, Y
通讯作者:
Ishino, Y