ArticleBiochemistry2005
Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
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- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Sirtuin 1-mediated deacetylation of XPA DNA repair protein enhances its interaction with ATR protein and promotes cAMP-induced DNA repair of UV damage.The Journal of biological chemistry · 2018Article
- A new structural insight into XPA-DNA interactions.Bioscience reports · 2014Article
- Progress and outlook in structural biology of large viral RNAs.Virus research · 2014Review
- Protein modification by adenine propenal.Chemical research in toxicology · 2014Article
- Investigation of stable and transient protein-protein interactions: Past, present, and future.Proteomics · 2013Review
- Mapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probe.Molecular & cellular proteomics : MCP · 2012Article
- Traveling-wave ion mobility mass spectrometry analysis of isomeric modified peptides arising from chemical cross-linking.Journal of the American Society for Mass Spectrometry · 2010Article
- 'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.Journal of the American Society for Mass Spectrometry · 2010Article
- Checkpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A.The Journal of biological chemistry · 2009Article
- Probing conformational changes of human DNA polymerase lambda using mass spectrometry-based protein footprinting.Journal of molecular biology · 2009Article
- Mass spectrometry-based footprinting of protein-protein interactions.Methods (San Diego, Calif.) · 2009Article
- Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein.The Journal of biological chemistry · 2008Article
- Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.Journal of the American Society for Mass Spectrometry · 2008Article
- DNA-dependent conformational changes in the Ku heterodimer.Biochemistry · 2008Article
- Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase.Biochemical and biophysical research communications · 2008Article
- Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding.The Journal of biological chemistry · 2008Article
- Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Biochemistry · 2007Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Human replication protein A (hRPA), a heterotrimeric single-stranded DNA (ssDNA) binding protein, is required for many cellular pathways including DNA damage repair, recombination, and replication as well as the ATR-mediated DNA damage response. While extensive effort has been devoted to understanding the structural relationships between RPA and ssDNA, information is currently limited to the RPA domains, the trimerization core, and a partial cocrystal structure. In this work, we employed a mass spectrometric protein footprinting method of single amino acid resolution to investigate the interactions of the entire heterotrimeric hRPA with ssDNA. In particular, we monitored surface accessibility of RPA lysines with NHS-biotin modification in the contexts of the free protein and the nucleoprotein complex. Our results not only indicated excellent agreement with the available crystal structure data for RPA70 DBD-AB-ssDNA complex but also revealed new protein contacts in the nucleoprotein complex. In addition to two residues, K263 and K343 of p70, previously identified by cocrystallography as direct DNA contacts, we observed protection of five additional lysines (K183, K259, K489, K577, and K588 of p70) upon ssDNA binding to RPA. Three residues, K489, K577, and K588, are located in ssDNA binding domain C and are likely to establish the direct contacts with cognate DNA. In contrast, no ssDNA-contacting lysines were identified in DBD-D. In addition, two lysines, K183 and K259, are positioned outside the putative ssDNA binding cleft. We propose that the protection of these lysines could result from the RPA interdomain structural reorganization induced by ssDNA binding.
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Registered trials
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