Linked Life Data

12139939

Source:http://linkedlifedata.com/resource/pubmed/id/12139939

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-7-25
pubmed:abstractText
The eukaryotic single-stranded DNA-binding protein, replication protein A (RPA), is essential for DNA replication, and plays important roles in DNA repair and DNA recombination. Rad52 and RPA, along with other members of the Rad52 epistasis group of genes, repair double-stranded DNA breaks (DSBs). Two repair pathways involve RPA and Rad52, homologous recombination and single-strand annealing. Two binding sites for Rad52 have been identified on RPA. They include the previously identified C-terminal domain (CTD) of RPA32 (residues 224-271) and the newly identified domain containing residues 169-326 of RPA70. A region on Rad52, which includes residues 218-303, binds RPA70 as well as RPA32. The N-terminal region of RPA32 does not appear to play a role in the formation of the RPA:Rad52 complex. It appears that the RPA32CTD can substitute for RPA70 in binding Rad52. Sequence homology between RPA32 and RPA70 was used to identify a putative Rad52-binding site on RPA70 that is located near DNA-binding domains A and B. Rad52 binding to RPA increases ssDNA affinity significantly. Mutations in DBD-D on RPA32 show that this domain is primarily responsible for the ssDNA binding enhancement. RPA binding to Rad52 inhibits the higher-order self-association of Rad52 rings. Implications for these results for the "hand-off" mechanism between protein-protein partners, including Rad51, in homologous recombination and single-strand annealing are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
321
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-48
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12139939-Amino Acid Sequence, pubmed-meshheading:12139939-Binding, Competitive, pubmed-meshheading:12139939-DNA, Single-Stranded, pubmed-meshheading:12139939-DNA Damage, pubmed-meshheading:12139939-DNA Repair, pubmed-meshheading:12139939-DNA Replication, pubmed-meshheading:12139939-DNA-Binding Proteins, pubmed-meshheading:12139939-Electrophoretic Mobility Shift Assay, pubmed-meshheading:12139939-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:12139939-Humans, pubmed-meshheading:12139939-Light, pubmed-meshheading:12139939-Macromolecular Substances, pubmed-meshheading:12139939-Molecular Sequence Data, pubmed-meshheading:12139939-Mutation, pubmed-meshheading:12139939-Osmolar Concentration, pubmed-meshheading:12139939-Precipitin Tests, pubmed-meshheading:12139939-Protein Binding, pubmed-meshheading:12139939-Protein Structure, Tertiary, pubmed-meshheading:12139939-Rad51 Recombinase, pubmed-meshheading:12139939-Rad52 DNA Repair and Recombination Protein, pubmed-meshheading:12139939-Replication Protein A, pubmed-meshheading:12139939-Scattering, Radiation, pubmed-meshheading:12139939-Simian virus 40, pubmed-meshheading:12139939-Surface Plasmon Resonance
pubmed:year
2002
pubmed:articleTitle
Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA.
pubmed:affiliation
Department of Chemistry, University of Toledo, 2801 West Bancroft Street, OH 43606-3390, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.