The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction.
The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction.
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古细菌 ATP 酶 PINA 通过其羧基末端 KH 结构域重塑和加工复制叉和霍利迪连接与解旋酶 Hjm 相互作用
DOI:
10.1093/nar/gky451
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发表时间:
2018-07-27
影响因子:
14.9
通讯作者:
Shen Y
中科院分区:
文献类型:
--
作者:
Zhai B;DuPrez K;Han X;Yuan Z;Ahmad S;Xu C;Gu L;Ni J;Fan L;Shen Y
Abstract PINA is a novel ATPase and DNA helicase highly conserved in Archaea, the third domain of life. The PINA from Sulfolobus islandicus (SisPINA) forms a hexameric ring in crystal and solution. The protein is able to promote Holliday junction (HJ) migration and physically and functionally interacts with Hjc, the HJ specific endonuclease. Here, we show that SisPINA has direct physical interaction with Hjm (Hel308a), a helicase presumably targeting replication forks. In vitro biochemical analysis revealed that Hjm, Hjc, and SisPINA are able to coordinate HJ migration and cleavage in a concerted way. Deletion of the carboxyl 13 amino acid residues impaired the interaction between SisPINA and Hjm. Crystal structure analysis showed that the carboxyl 70 amino acid residues fold into a type II KH domain which, in other proteins, functions in binding RNA or ssDNA. The KH domain not only mediates the interactions of PINA with Hjm and Hjc but also regulates the hexameric assembly of PINA. Our results collectively suggest that SisPINA, Hjm and Hjc work together to function in replication fork regression, HJ formation and HJ cleavage.
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影响因子:
3.8
作者:
Hong, Ye;Chu, Mingzhu;Shen, Yulong
通讯作者:
Shen, Yulong
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:
4.8
作者:
Fujikane, R;Komori, K;Ishino, Y
通讯作者:
Ishino, Y
影响因子:
4.8
作者:
Gupta, Sankalp;Yeeles, Joseph T. P.;Marians, Kenneth J.
通讯作者:
Marians, Kenneth J.
影响因子:
2.1
作者:
Fujikane, R;Shinagawa, H;Ishino, Y
通讯作者:
Ishino, Y