ArticleNucleic acids research2017
Structural basis for the functional role of the Shu complex in homologous recombination.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- SPIDR is required for homologous recombination during mammalian meiosis.Nucleic acids research · 2023Article
- Distinct pathways of homologous recombination controlled by the SWS1-SWSAP1-SPIDR complex.Nature communications · 2021Article
- Review
- Conditional knockout of RAD51-related genes in Leishmania major reveals a critical role for homologous recombination during genome replication.PLoS genetics · 2020Article
- Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020Review
- Advances in genome editing through control of DNA repair pathways.Nature cell biology · 2019Review
- The Rad51 paralogs facilitate a novel DNA strand specific damage tolerance pathway.Nature communications · 2019Article
- Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase.Nature communications · 2019Article
- Lsm12 Mediates Deubiquitination of DNA Polymerase η To HelpApplied and environmental microbiology · 2019Article
- RAD-ical New Insights into RAD51 Regulation.Genes · 2018Review
- Biochemical attributes of mitotic and meiotic presynaptic complexes.DNA repair · 2018Review
- Shu complex SWS1-SWSAP1 promotes early steps in mouse meiotic recombination.Nature communications · 2018Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Shu complex, a conserved regulator consisting of Csm2, Psy3, Shu1 and Shu2 in budding yeast, plays an important role in the assembly of the Rad51-ssDNA filament in homologous recombination. However, the molecular basis for the assembly of the Shu complex and its functional role in DNA repair is still elusive. Here, we report the crystal structure of the yeast Shu complex, revealing that Csm2, Psy3, Shu1 and Shu2 interact with each other in sequence to form a V-shape overall structure. Shu1 adopts a structure resembling the ATPase core domain of Rad51 and represents a new Rad51 paralog. Shu2 assumes a novel structural fold consisting of a conserved zinc-finger containing SWIM domain and a small insertion domain. The functional roles of the key residues are validated using mutagenesis and in vitro pull-down and in vivo yeast growth studies. Structural analysis together with available biological data identifies two potential DNA-binding sites, one of which might be responsible for binding the ssDNA region of the 3'-overhang DNA and the other for the dsDNA region. Collectively, these findings reveal the molecular basis for the assembly of the Shu complex and shed new insight on its functional role in homologous recombination.
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