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• W2031039047 endingPage "3936" @default.
• W2031039047 startingPage "3932" @default.
• W2031039047 abstract "<i>R</i>eplication <i>p</i>rotein <i>A</i> (RPA) is a conserved nuclear single-stranded DNA (ssDNA)-binding protein. Human RPA (hRPA) comprises three subunits of approximately 70, 32, and 14 kDa (hRPA70, hRPA32 and hRPA14). RPA is known to bind ssDNA through two ssDNA-binding domains in the RPA70 subunit. Here, we demonstrate that the complex of hRPA32 and hRPA14 has an ssDNA-binding domain. Limited proteolysis of the hRPA14·32 complex defined a core dimer composed of the central region of hRPA32 (amino acids 43–171) and RPA14. The core dimer bound ssDNA with an affinity of approximately 10–50 μm, which is at least 100-fold more avid than the DNA-binding affinity of the intact dimer. Analysis of the predicted secondary structure of hRPA32 suggests that amino acids 63–150 of hRPA32 form an ssDNA-binding domain similar in structure to each of those in hRPA70. The complex of hRPA14 and hRPA32-(43–171) in turn formed a trimeric complex with the C-terminal region of hRPA70 (amino acids 436–616). The ssDNA-binding affinity of this trimeric complex was 3 to 5-fold higher than hRPA14·32-(43–171) alone, suggesting a role for the C terminus of hRPA70 in ssDNA binding." @default.
• W2031039047 created "2016-06-24" @default.
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• W2031039047 creator A5070600206 @default.
• W2031039047 date "1998-02-01" @default.
• W2031039047 modified "2023-10-12" @default.
• W2031039047 title "The RPA32 Subunit of Human Replication Protein A Contains a Single-stranded DNA-binding Domain" @default.
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• W2031039047 doi "https://doi.org/10.1074/jbc.273.7.3932" @default.
• W2031039047 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9461578" @default.
• W2031039047 hasPublicationYear "1998" @default.
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