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Human replication protein A (RPA) is a three subunit protein
complex involved in DNA replication, repair, and recombination. We
investigated the role of the 34-kDa subunit (p34) of RPA in DNA
replication by generating a series of p34 mutants. While deletion of
the N-terminal domain of p34 prevented its phosphorylation by both
cyclin-dependent kinase (Cdk) and DNA-dependent kinase, a double point
mutant that lacks the major phosphorylation sites for Cdk could be
phosphorylated by DNA-dependent kinase. In simian virus 40
(SV40) DNA replication, RPA containing either of these mutants
functioned as efficiently as wild-type RPA. However, mutant RPA
containing C-terminally deleted p34 was only marginally active. This
indicates that the C-terminal region, but not the phosphorylation
domain of p34, is necessary for RPA function in DNA replication.
Furthermore, RPA containing the C-terminally deleted p34 mutant could
stimulate DNA polymerase
Volume 270,
Number 21,
Issue of May 26, pp. 12801-12807, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
, and bind to single-stranded DNAs but
was limited in its ability to unwind DNA or interact with SV40 large T
antigen (T Ag). These results suggest that RPA p34 interacts with SV40
T Ag during the initiation of SV40 DNA replication and may be necessary
for DNA unwinding.
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