ArticleNucleic acids research2015
The N-terminus of RPA large subunit and its spatial position are important for the 5'->3' resection of DNA double-strand breaks.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Distinct RPA domains promote recruitment and the helicase-nuclease activities of Dna2.Nature communications · 2021Article
- Emerging roles of non-histone protein crotonylation in biomedicine.Cell & bioscience · 2021Review
- The Bloom syndrome complex senses RPA-coated single-stranded DNA to restart stalled replication forks.Nature communications · 2021Article
- Global crotonylome reveals CDYL-regulated RPA1 crotonylation in homologous recombination-mediated DNA repair.Science advances · 2020Article
- Investigation of the core binding regions of human Werner syndrome and Fanconi anemia group J helicases on replication protein A.Scientific reports · 2019Article
- Multiple RPAs make WRN syndrome protein a superhelicase.Nucleic acids research · 2018Article
- Dna2 initiates resection at clean DNA double-strand breaks.Nucleic acids research · 2017Article
- Interactive Roles of DNA Helicases and Translocases with the Single-Stranded DNA Binding Protein RPA in Nucleic Acid Metabolism.International journal of molecular sciences · 2017Review
- CDK1 phosphorylates WRN at collapsed replication forks.Nature communications · 2016Article
- Sharpening the ends for repair: mechanisms and regulation of DNA resection.Acta biochimica et biophysica Sinica · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The first step of homology-dependent repair of DNA double-strand breaks (DSBs) is the resection of the 5' strand to generate 3' ss-DNA. Of the two major nucleases responsible for resection, EXO1 has intrinsic 5'->3' directionality, but DNA2 does not. DNA2 acts with RecQ helicases such as the Werner syndrome protein (WRN) and the heterotrimeric eukaryotic ss-DNA binding protein RPA. We have found that the N-terminus of the RPA large subunit (RPA1N) interacts with both WRN and DNA2 and is essential for stimulating WRN's 3'->5' helicase activity and DNA2's 5'->3' ss-DNA exonuclease activity. A mutant RPA complex that lacks RPA1N is unable to support resection in Xenopus egg extracts and human cells. Furthermore, relocating RPA1N to the middle subunit but not to the small subunit causes severe defects in stimulating DNA2 and WRN and in supporting resection. Together, these findings suggest that RPA1N and its spatial position are critical for restricting the directionality of the WRN-DNA2 resection pathway.
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Registered trials
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