globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1812753115
论文题名:
Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation
作者: Lu C.-H.; Yeh H.-Y.; Su G.-C.; Ito K.; Kurokawa Y.; Iwasaki H.; Chi P.; Li H.-W.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:43
起始页码: E10059
结束页码: E10068
语种: 英语
英文关键词: Homologous recombination ; Rad51 ; Single-molecule microscopy ; Swi5-Sfr1
Scopus关键词: fungal protein ; nucleic acid binding protein ; Rad51 protein ; Sfr1 protein ; Swi5 protein ; unclassified drug ; DNA ; nuclear protein ; nucleoprotein ; Rad51 protein ; Rad51 protein, mouse ; Sfr1 protein, mouse ; Swi5 protein, mouse ; Article ; concentration response ; fission yeast ; fluorescence resonance energy transfer ; homologous recombination ; nonhuman ; nucleoprotein filament assembly ; priority journal ; protein assembly ; protein binding ; protein function ; protein induction, synthesis and modification ; protein nucleation ; protein stability ; regulatory mechanism ; animal ; metabolism ; mouse ; physiology ; Schizosaccharomyces ; Animals ; DNA ; Homologous Recombination ; Mice ; Nuclear Proteins ; Nucleoproteins ; Rad51 Recombinase ; Schizosaccharomyces
英文摘要: Eukaryotic Rad51 protein is essential for homologous-recombination repair of DNA double-strand breaks. Rad51 recombinases first assemble onto single-stranded DNA to forma nucleoprotein filament, required for function in homology pairing and strand exchange. This filament assembly is the first regulation step in homologous recombination. Rad51 nucleation is kinetically slow, and several accessory factors have been identified to regulate this step. Swi5-Sfr1 (S5S1) stimulates Rad51-mediated homologous recombination by stabilizing Rad51 nucleoprotein filaments, but the mechanism of stabilization is unclear. We used single-molecule tethered particle motion experiments to show that mouse S5S1 (mS5S1) efficiently stimulates mouse RAD51 (mRAD51) nucleus formation and inhibits mRAD51 dissociation from filaments. We also used single-molecule fluorescence resonance energy transfer experiments to show that mS5S1 promotes stable nucleus formation by specifically preventing mRAD51 dissociation. This leads to a reduction of nucleation size from three mRAD51 to two mRAD51 molecules in the presence of mS5S1. Compared with mRAD51, fission yeast Rad51 (SpRad51) exhibits fast nucleation but quickly dissociates from the filament. SpS5S1 specifically reduces SpRad51 disassembly to maintain a stable filament. These results clearly demonstrate the conserved function of S5S1 by primarily stabilizing Rad51 on DNA, allowing both the formation of the stable nucleus and the maintenance of filament length. © 2018 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163649
Appears in Collections:气候变化与战略

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作者单位: Lu, C.-H., Department of Chemistry, National Taiwan University, Taipei, 10617, Taiwan; Yeh, H.-Y., Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan; Su, G.-C., Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan; Ito, K., Institute of Innovative Research, Tokyo Institute of Technology, Tokyo, 152-8550, Japan; Kurokawa, Y., Institute of Innovative Research, Tokyo Institute of Technology, Tokyo, 152-8550, Japan; Iwasaki, H., Institute of Innovative Research, Tokyo Institute of Technology, Tokyo, 152-8550, Japan; Chi, P., Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan, Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan; Li, H.-W., Department of Chemistry, National Taiwan University, Taipei, 10617, Taiwan, Center for Frontier Research, National Institute of Genetics, Mishima, 411-8510, Japan

Recommended Citation:
Lu C.-H.,Yeh H.-Y.,Su G.-C.,et al. Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(43)
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