ArticleNucleic acids research2016
Involvement of budding yeast Rad5 in translesion DNA synthesis through physical interaction with Rev1.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 79 citations in OpenAlex.
- Increased replication-associated single-stranded DNA promotes formaldehyde-induced mutagenesis.bioRxiv : the preprint server for biology · 2026Article
- Rad51 determines pathway usage in post-replication repair.Nature communications · 2026Article
- Budding Yeast Ubiquitin Ligases Rad5 and Rad18 Bind a Novel PCNA Surface, which Is Required for their Functions in DNA-Damage Tolerance.International journal of biological sciences · 2026Article
- The DNA damage tolerance factor Rad5 and telomere replication.Current genetics · 2025Review
- Protein Assemblies in Translesion Synthesis.Genes · 2024Review
- Spatial regulation of DNA damage tolerance protein Rad5 interconnects genome stability maintenance and proteostasis networks.Nucleic acids research · 2024Article
- Helicase activities of Rad5 and Rrm3 genetically interact in the prevention of recombinogenic DNA lesions in Saccharomyces cerevisiae.DNA repair · 2023Article
- Polymorphism ofInternational journal of molecular sciences · 2023Article
- Article
- Implications of Translesion DNA Synthesis Polymerases on Genomic Stability and Human Health.Molecular and cellular biology · 2023Article
- Post-Translational Modifications of PCNA: Guiding for the Best DNA Damage Tolerance Choice.Journal of fungi (Basel, Switzerland) · 2022Review
- Rad5 participates in lesion bypass through its Rev1-binding and ubiquitin ligase domains, but not through its helicase function.Frontiers in molecular biosciences · 2022Article
- The Conceivable Functions of Protein Ubiquitination and Deubiquitination in Reproduction.Frontiers in physiology · 2022Review
- Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors of Mismatch Repair.Frontiers in cell and developmental biology · 2022Article
- A role for Rad5 in ribonucleoside monophosphate (rNMP) tolerance.Life science alliance · 2021Article
- Structural basis for the multi-activity factor Rad5 in replication stress tolerance.Nature communications · 2021Article
- Yeast DNA polymerase η possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities.DNA repair · 2020Article
- Distinct requirements for budding yeast Rev1 and Polη in translesion DNA synthesis across different types of DNA damage.Current genetics · 2020Article
- Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair.Nature communications · 2020Article
- Regulation of the abundance of Y-family polymerases in the cell cycle of budding yeast in response to DNA damage.Current genetics · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA damage tolerance (DDT) is responsible for genomic stability and cell viability by bypassing the replication block. In Saccharomyces cerevisiae DDT employs two parallel branch pathways to bypass the DNA lesion, namely translesion DNA synthesis (TLS) and error-free lesion bypass, which are mediated by sequential modifications of PCNA. Rad5 has been placed in the error-free branch of DDT because it contains an E3 ligase domain required for PCNA polyubiquitination. Rad5 is a multi-functional protein and may also play a role in TLS, since it interacts with the TLS polymerase Rev1. In this study we mapped the Rev1-interaction domain in Rad5 to the amino acid resolution and demonstrated that Rad5 is indeed involved in TLS possibly through recruitment of Rev1. Genetic analyses show that the dual functions of Rad5 can be separated and reconstituted. Crystal structure analysis of the Rad5-Rev1 interaction reveals a consensus RFF motif in the Rad5 N-terminus that binds to a hydrophobic pocket within the C-terminal domain of Rev1 that is highly conserved in eukaryotes. This study indicates that Rad5 plays a critical role in pathway choice between TLS and error-free DDT.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.