ArticleGenetics2015
Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.
Article in Genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Secondary Somatic Mutations RestoringCancer discovery · 2017Trial
- Genome Wide Identification and Characterization of LIM Domain Associated Gene Superfamily in Common Bean (International journal of genomics · 2025Article
- Evolutionary rate covariation is pervasive between glycosylation pathways and points to potential disease modifiers.PLoS genetics · 2024Article
- The human Shu complex promotes RAD51 activity by modulating RPA dynamics on ssDNA.Nature communications · 2024Article
- FIGNL1-FIRRM is essential for meiotic recombination and prevents DNA damage-independent RAD51 and DMC1 loading.Nature communications · 2024Article
- Repair of DNA double-strand breaks in plant meiosis: role of eukaryotic RecA recombinases and their modulators.Plant reproduction · 2023Review
- The conserved Pelado/ZSWIM8 protein regulates actin dynamics by promoting linear actin filament polymerization.Life science alliance · 2022Article
- RAD51 paralog function in replicative DNA damage and tolerance.Current opinion in genetics & development · 2021Review
- The Shu complex prevents mutagenesis and cytotoxicity of single-strand specific alkylation lesions.eLife · 2021Article
- Distinct pathways of homologous recombination controlled by the SWS1-SWSAP1-SPIDR complex.Nature communications · 2021Article
- Novel ACE2 protein interactions relevant to COVID-19 predicted by evolutionary rate correlations.PeerJ · 2021Article
- The human Shu complex functions with PDS5B and SPIDR to promote homologous recombination.Nucleic acids research · 2019Article
- Evolution-based screening enables genome-wide prioritization and discovery of DNA repair genes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Rad51 paralogs facilitate a novel DNA strand specific damage tolerance pathway.Nature communications · 2019Article
- Evolutionary rate covariation analysis of E-cadherin identifies Raskol as a regulator of cell adhesion and actin dynamics in Drosophila.PLoS genetics · 2019Article
- Shu complex SWS1-SWSAP1 promotes early steps in mouse meiotic recombination.Nature communications · 2018Article
- A Genome-Wide Association Study in Hispanics/Latinos Identifies Novel Signals for Lung Function. The Hispanic Community Health Study/Study of Latinos.American journal of respiratory and critical care medicine · 2018Article
- Structural basis for the functional role of the Shu complex in homologous recombination.Nucleic acids research · 2017Article
- Review
- A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling.Molecular cell · 2016Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae Shu2 protein is an important regulator of Rad51, which promotes homologous recombination (HR). Shu2 functions in the Shu complex with Shu1 and the Rad51 paralogs Csm2 and Psy3. Shu2 belongs to the SWS1 protein family, which is characterized by its SWIM domain (CXC...Xn...CXH), a zinc-binding motif. In humans, SWS1 interacts with the Rad51 paralog SWSAP1. Using genetic and evolutionary analyses, we examined the role of the Shu complex in mitotic and meiotic processes across eukaryotic lineages. We provide evidence that the SWS1 protein family contains orthologous genes in early-branching eukaryote lineages (e.g., Giardia lamblia), as well as in multicellular eukaryotes including Caenorhabditis elegans and Drosophila melanogaster. Using sequence analysis, we expanded the SWIM domain to include an invariant alanine three residues after the terminal CXH motif (CXC…Xn…CXHXXA). We found that the SWIM domain is conserved in all eukaryotic orthologs, and accordingly, in vivo disruption of the invariant residues within the canonical SWIM domain inhibits DNA damage tolerance in yeast and protein-protein interactions in yeast and humans. Furthermore, using evolutionary analyses, we found that yeast and Drosophila Shu2 exhibit strong coevolutionary signatures with meiotic proteins, and in yeast, its disruption leads to decreased meiotic progeny. Together our data indicate that the SWS1 family is an ancient and highly conserved eukaryotic regulator of meiotic and mitotic HR.
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Registered trials
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