ArticleBiochemistry2013
Structure and functional analysis of the BRCT domain of translesion synthesis DNA polymerase Rev1.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Opposing regulation by Rev1 of DNA polymerase zeta activity on damaged versus undamaged DNA.Nucleic acids research · 2026Article
- Opposing regulation by Rev1 of DNA polymerase zeta activity on damaged versus undamaged DNA.bioRxiv : the preprint server for biology · 2026Article
- Domain-Specific DNA Binding Activities of BRCA1 Reveal Substrate Preferences for Homologous Recombination and Telomere Regulation.Biochemistry · 2025Article
- Cryo-EM structure of the Rev1-Polζ holocomplex reveals the mechanism of their cooperativity in translesion DNA synthesis.Nature structural & molecular biology · 2024Article
- Protein Assemblies in Translesion Synthesis.Genes · 2024Review
- Post-Translational Modifications of PCNA: Guiding for the Best DNA Damage Tolerance Choice.Journal of fungi (Basel, Switzerland) · 2022Review
- Translesion synthesis polymerases are dispensable for C. elegans reproduction but suppress genome scarring by polymerase theta-mediated end joining.PLoS genetics · 2020Article
- Sml1 Inhibits the DNA Repair Activity of Rev1 in Saccharomyces cerevisiae during Oxidative Stress.Applied and environmental microbiology · 2020Article
- The Rev1-Polζ translesion synthesis mutasome: Structure, interactions and inhibition.The Enzymes · 2019Review
- Modeling Conformationally Flexible Proteins With X-ray Scattering and Molecular Simulations.Computational and structural biotechnology journal · 2019Review
- Structural Basis for the Interaction of Mutasome Assembly Factor REV1 with Ubiquitin.Journal of molecular biology · 2018Article
- An overview of Y-Family DNA polymerases and a case study of human DNA polymerase η.Biochemistry · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Translesion synthesis (TLS) is a pathway in which specialized, low-fidelity DNA polymerases are used to overcome replication blocks caused by DNA damage. The use of this pathway often results in somatic mutations that can drive carcinogenesis. Rev1 is a TLS polymerase found in all eukaryotes that plays a pivotal role in mediating DNA damage-induced mutagenesis. It possesses a BRCA1 C-terminal (BRCT) domain that is required for its function. The rev1-1 allele encodes a mutant form of Rev1 with a G193R substitution in this domain, which reduces the level of DNA damage-induced mutagenesis. Despite its clear importance in mutagenic TLS, the role of the BRCT domain is unknown. Here, we report the X-ray crystal structure of the yeast Rev1 BRCT domain and show that substitutions in residues constituting its phosphate-binding pocket do not affect mutagenic TLS. This suggests that the role of the Rev1 BRCT domain is not to recognize phosphate groups on protein binding partners or on DNA. We also found that residue G193 is located in a conserved turn region of the BRCT domain, and our in vivo and in vitro studies suggest that the G193R substitution may disrupt Rev1 function by destabilizing the fold of the BRCT domain.
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Registered trials
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