ArticleMethods in molecular biology (Clifton, N.J.)2021
Generation of Fluorescent Versions of Saccharomyces cerevisiae RPA to Study the Conformational Dynamics of Its ssDNA-Binding Domains.
Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Mechanism of Rad51 filament formation by Rad52 and Rad55-Rad57 in homologous recombination.Nature communications · 2025Article
- Human hnRNPA1 reorganizes telomere-bound replication protein A.Nucleic acids research · 2024Article
- Rad52 sorts and stacks Rad51 at the DNA junction to promote homologous recombination.bioRxiv : the preprint server for biology · 2024Article
- Generation of site-specifically labelled fluorescent human XPA to investigate DNA binding dynamics during nucleotide excision repair.Methods (San Diego, Calif.) · 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
- Fluorescent human RPA to track assembly dynamics on DNA.bioRxiv : the preprint server for biology · 2023Article
- An Aurora B-RPA signaling axis secures chromosome segregation fidelity.Nature communications · 2023Article
- Site-specific labeling of SBDS to monitor interactions with the 60S ribosomal subunit.Methods (San Diego, Calif.) · 2023Article
- Rtt105 regulates RPA function by configurationally stapling the flexible domains.Nature communications · 2022Article
- Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Replication protein A (RPA) is an essential single-stranded DNA (ssDNA)-binding protein that sequesters ssDNA and protects it from nucleolytic degradation. The RPA-ssDNA nucleoprotein acts as a hub to recruit over two dozen DNA metabolic enzymes onto ssDNA to coordinate DNA replication, repair, and recombination. RPA functions as a heterotrimer composed of RPA70, RPA32, and RPA14 subunits and has multiple DNA-binding and protein-interaction domains. Several of these domains are connected by disordered linkers allowing RPA to adopt a wide variety of conformations on ssDNA. Here we describe a fluorescence-based tool to monitor the dynamics of select DNA-binding domains of RPA. Noncanonical amino acids are utilized to site-specifically engineer fluorescent probes in Saccharomyces cerevisiae RPA heterologously expressed in BL21 (DE3) and its derivatives. A procedure to synthesize 4-azido-L-phenylalanine (4AZP), a noncanonical amino acid, is also described. Sites for fluorophore positioning that produce a measurable change in fluorescence upon binding to ssDNA are detailed. This fluorescence enhancement through noncanonical amino acid (FEncAA) approach can also be applied to other DNA-binding proteins to investigate the dynamics of protein-nucleic acid interactions.
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