ArticleBiochemistry2010
Structural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scattering.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- Fluorescent human RPA to track assembly dynamics on DNA.Methods (San Diego, Calif.) · 2024Article
- Review
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Fluorescent human RPA to track assembly dynamics on DNA.bioRxiv : the preprint server for biology · 2023Article
- Three-Dimensional Modeling of CpG DNA Binding with Matrix Lumican Shows Leucine-Rich Repeat Motif Involvement as in TLR9-CpG DNA Interactions.International journal of molecular sciences · 2023Article
- An Aurora B-RPA signaling axis secures chromosome segregation fidelity.Nature communications · 2023Article
- Interdomain dynamics in human Replication Protein A regulates kinetics and thermodynamics of its binding to ssDNA.PloS one · 2023Article
- EXO5-DNA structure and BLM interactions direct DNA resection critical for ATR-dependent replication restart.Molecular cell · 2021Article
- Hydrogen-deuterium exchange reveals a dynamic DNA-binding map of replication protein A.Nucleic acids research · 2021Article
- Decoding Cancer Variants of Unknown Significance for Helicase-Nuclease-RPA Complexes Orchestrating DNA Repair During Transcription and Replication.Frontiers in molecular biosciences · 2021Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Human replication protein A induces dynamic changes in single-stranded DNA and RNA structures.The Journal of biological chemistry · 2019Article
- Dynamics and selective remodeling of the DNA-binding domains of RPA.Nature structural & molecular biology · 2019Article
- Analysis and prediction of single-stranded and double-stranded DNA binding proteins based on protein sequences.BMC bioinformatics · 2017Article
- Functional dynamics in replication protein A DNA binding and protein recruitment domains.Structure (London, England : 1993) · 2015Article
- Dimerization and phosphatase activity of calcyclin-binding protein/Siah-1 interacting protein: the influence of oxidative stress.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Characteristics and concepts of dynamic hub proteins in DNA processing machinery from studies of RPA.Progress in biophysics and molecular biology · 2015Review
- Architecture and ssDNA interaction of the Timeless-Tipin-RPA complex.Nucleic acids research · 2014Article
- Identification of single-stranded and double-stranded DNA binding proteins based on protein structure.BMC bioinformatics · 2014Article
- A new structural framework for integrating replication protein A into DNA processing machinery.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Replication protein A (RPA) is the primary eukaryotic single-stranded DNA (ssDNA) binding protein utilized in diverse DNA transactions in the cell. RPA is a heterotrimeric protein with seven globular domains connected by flexible linkers, which enable substantial interdomain motion that is essential to its function. Small angle X-ray scattering (SAXS) experiments with two multidomain constructs from the N-terminus of the large subunit (RPA70) were used to examine the structural dynamics of these domains and their response to the binding of ssDNA. The SAXS data combined with molecular dynamics simulations reveal substantial interdomain flexibility for both RPA70AB (the tandem high-affinity ssDNA binding domains A and B connected by a 10-residue linker) and RPA70NAB (RPA70AB extended by a 70-residue linker to the RPA70N protein interaction domain). Binding of ssDNA to RPA70NAB reduces the interdomain flexibility between the A and B domains but has no effect on RPA70N. These studies provide the first direct measurements of changes in orientation of these three RPA domains upon binding ssDNA. The results support a model in which RPA70N remains structurally independent of RPA70AB in the DNA-bound state and therefore freely available to serve as a protein recruitment module.
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Registered trials
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.