ArticleStructure (London, England : 1993)2015
Functional dynamics in replication protein A DNA binding and protein recruitment domains.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- RPA-ssDNA co-phase separation facilitates RAD51 enrichment during homologous recombination.Nucleic acids research · 2026Article
- Human hnRNPA1 reorganizes telomere-bound replication protein A.Nucleic acids research · 2024Article
- Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rapid Long-distance Migration of RPA on Single Stranded DNA Occurs Through Intersegmental Transfer Utilizing Multivalent Interactions.Journal of molecular biology · 2024Article
- Fluorescent human RPA to track assembly dynamics on DNA.Methods (San Diego, Calif.) · 2024Article
- Review
- Fluorescent human RPA to track assembly dynamics on DNA.bioRxiv : the preprint server for biology · 2023Article
- Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.bioRxiv : the preprint server for biology · 2023Article
- A DNA damage-induced phosphorylation circuit enhances Mec1Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Phase separation properties of RPA combine high-affinity ssDNA binding with dynamic condensate functions at telomeres.Nature structural & molecular biology · 2023Article
- Interdomain dynamics in human Replication Protein A regulates kinetics and thermodynamics of its binding to ssDNA.PloS one · 2023Article
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Review
- KERA: analysis tool for multi-process, multi-state single-molecule data.Nucleic acids research · 2021Article
- Hydrogen-deuterium exchange reveals a dynamic DNA-binding map of replication protein A.Nucleic acids research · 2021Article
- Generation of Fluorescent Versions of Saccharomyces cerevisiae RPA to Study the Conformational Dynamics of Its ssDNA-Binding Domains.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Dynamic elements of replication protein A at the crossroads of DNA replication, recombination, and repair.Critical reviews in biochemistry and molecular biology · 2020Review
- Structure-Guided Optimization of Replication Protein A (RPA)-DNA Interaction Inhibitors.ACS medicinal chemistry letters · 2020Article
- Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020Review
- Human replication protein A induces dynamic changes in single-stranded DNA and RNA structures.The Journal of biological chemistry · 2019Article
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7 authors.
Funding
Abstract
Replication Protein A (RPA) is an essential scaffold for many DNA processing machines; its function relies on its modular architecture. Here, we report (15)N-nuclear magnetic resonance heteronuclear relaxation analysis to characterize the movements of single-stranded (ss) DNA binding and protein interaction modules in the RPA70 subunit. Our results provide direct evidence for coordination of the motion of the tandem RPA70AB ssDNA binding domains. Moreover, binding of ssDNA substrate is found to cause dramatic reorientation and full coupling of inter-domain motion. In contrast, the RPA70N protein interaction domain remains structurally and dynamically independent of RPA70AB regardless of binding of ssDNA. This autonomy of motion between the 70N and 70AB modules supports a model in which the two binding functions of RPA are mediated fully independently, but remain differentially coordinated depending on the length of their flexible tethers. A critical role for linkers between the globular domains in determining the functional dynamics of RPA is proposed.
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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.