ArticleNucleic acids research2005
The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 79 citations in OpenAlex.
- Helicase activities of Rad5 and Rrm3 genetically interact in the prevention of recombinogenic DNA lesions in Saccharomyces cerevisiae.DNA repair · 2023Article
- Fork-Remodeling Helicase Rad5 Preferentially Reverses Replication Forks with Gaps in the Leading Strand.Journal of molecular biology · 2023Article
- Snf2 Proteins Are Required to Generate Gamete Pronuclei inMicroorganisms · 2022Article
- Linkage reprogramming by tailor-made E3s reveals polyubiquitin chain requirements in DNA-damage bypass.Molecular cell · 2022Article
- Rad5 participates in lesion bypass through its Rev1-binding and ubiquitin ligase domains, but not through its helicase function.Frontiers in molecular biosciences · 2022Article
- Effects of chain length and geometry on the activation of DNA damage bypass by polyubiquitylated PCNA.Nucleic acids research · 2020Article
- Review
- Rad5 dysregulation drives hyperactive recombination at replication forks resulting in cisplatin sensitivity and genome instability.Nucleic acids research · 2019Article
- Regulation of HLTF-mediated PCNA polyubiquitination by RFC and PCNA monoubiquitination levels determines choice of damage tolerance pathway.Nucleic acids research · 2018Article
- BothAIMS genetics · 2017Article
- Involvement of budding yeast Rad5 in translesion DNA synthesis through physical interaction with Rev1.Nucleic acids research · 2016Article
- Identification of novel small ncRNAs in pollen of tomato.BMC genomics · 2015Article
- Concerted and differential actions of two enzymatic domains underlie Rad5 contributions to DNA damage tolerance.Nucleic acids research · 2015Article
- Regulation of Elg1 activity by phosphorylation.Cell cycle (Georgetown, Tex.) · 2015Article
- Regulation of the DNA damage response by ubiquitin conjugation.Frontiers in genetics · 2015Review
- Essential domains of Schizosaccharomyces pombe Rad8 required for DNA damage response.G3 (Bethesda, Md.) · 2014Article
- Post-translational modifications of proliferating cell nuclear antigen: A key signal integrator for DNA damage response (Review).Oncology letters · 2014Article
- Rad5-dependent DNA repair functions of the Saccharomyces cerevisiae FANCM protein homolog Mph1.The Journal of biological chemistry · 2012Article
- Helicase-like transcription factor confers radiation resistance in cervical cancer through enhancing the DNA damage repair capacity.Journal of cancer research and clinical oncology · 2011Article
- Elg1, an alternative subunit of the RFC clamp loader, preferentially interacts with SUMOylated PCNA.The EMBO journal · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tolerance to replication-blocking DNA lesions is achieved by means of ubiquitylation of PCNA, the processivity clamp for replicative DNA polymerases, by components of the RAD6 pathway. In the yeast Saccharomyces cerevisiae the ubiquitin ligase (E3) responsible for polyubiquitylation of the clamp is the RING finger protein Rad5p. Interestingly, the RING finger, responsible for the protein's E3 activity, is embedded in a conserved DNA-dependent ATPase domain common to helicases and chromatin remodeling factors of the SWI/SNF family. Here, we demonstrate that the Rad5p ATPase domain provides the basis for a function of the protein in DNA double-strand break repair via a RAD52- and Ku-independent pathway mediated by the Mre11/Rad50/Xrs2 protein complex. This activity is distinct and separable from the contribution of the RING domain to ubiquitin conjugation to PCNA. Moreover, we show that the Rad5 protein physically associates with the single-stranded DNA regions at a processed double-strand break in vivo. Our observations suggest that Rad5p is a multifunctional protein that--by means of independent enzymatic activities inherent in its RING and ATPase domains--plays a modulating role in the coordination of repair events and replication fork progression in response to various different types of DNA lesions.
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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.