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J Biol Chem, Vol. 273, Issue 7, 3932-3936, February 13, 1998
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, and§
From the Replication protein
A (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.
Ontario Cancer Institute, Department of
Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9,
Canada, the § Department of Medical Genetics and
Microbiology, Medical Sciences Building, University of Toronto,
Toronto, Ontario M5S1A8, Canada, and the Banting and Best
Department of Medical Research, C. H. Best Institute, University of
Toronto, Toronto, Ontario M5G 1L6, Canada
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