A Holliday junction resolvase from Pyrococcus furiosus:: Functional similarity to Escherichia coli RuvC provides evidence for conserved mechanism of homologous recombination in Bacteria, Eukarya, and Archaea

被引:96
作者
Komori, K
Sakae, S
Shinagawa, H
Morikawa, K
Ishino, Y [1 ]
机构
[1] Biomol Engn Res Inst, Dept Mol Biol, Osaka 5650874, Japan
[2] Biomol Engn Res Inst, Dept Biol Struct, Osaka 5650874, Japan
[3] Osaka Univ, Microbial Dis Res Inst, Dept Mol Microbiol, Osaka 5650871, Japan
关键词
DNA recombination; hyperthermophile;
D O I
10.1073/pnas.96.16.8873
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The Holliday junction is an essential intermediate of homologous recombination, RecA of Bacteria, Rad51 of Eukarya, and RadA of Archaea are structural and functional homologs, These proteins play a pivotal role in the formation of Holliday junctions from two homologous DNA duplexes. RuvC is a specific endonuclease that resolves Holliday junctions in Bacteria. A Holliday junction-resolving activity has been found in both yeast and mammalian cells, To examine whether the paradigm of homologous recombination apply to Archaea, we assayed and found the activity to resolve a synthetic Holliday junction in crude extract of Pyrococcus furiosus cells. The gene, hjc (Holliday junction cleavage), encodes a protein composed of 123 amino acids, whose sequence is not similar to that of any proteins with known function. However, all four archaea, whose total genome sequences have been published, have the homologous genes. The purified Njc protein cleaved the recombination intermediates formed by RecA in vitro. These results support the notion that the formation and resolution of Holliday junction is the common mechanism of homologous recombination in the three domains of life.
引用
收藏
页码:8873 / 8878
页数:6
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