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J. Biol. Chem., Vol. 269, Issue 15, 11121-11132, Apr, 1994
LA Henricksen, CB Umbricht and MS Wold
Replication protein A (RPA) is a multisubunit, single-stranded DNA- binding
protein that is absolutely required for replication of SV40 DNA. The three
cDNAs encoding the subunits of human replication protein A (70, 32, and 14
kDa) have been expressed individually and in combination in Escherichia
coli. When subunits were expressed individually, appropriately sized
polypeptides were synthesized, but were found to be either insoluble or
aggregated with other proteins. We examined the interactions between
individual RPA subunits by expressing pairs of subunits and determining if
they formed stable complexes. Only the 32- and 14-kDa subunits formed a
soluble complex when coexpressed. This complex was purified and
characterized. The 32-14 kDa subcomplex did not have any effect on DNA
replication and was not phosphorylated efficiently in vitro. We believe
that the 32.14-kDa subcomplex may be a precursor in the assembly of the
complete RPA complex. Coexpression of all three subunits of RPA resulted in
a significant portion of each polypeptide forming a soluble complex. We
have purified recombinant RPA complex from E. coli and demonstrated that it
has properties similar to those of human RPA. Recombinant human RPA has the
same subunit composition and the same activities as the authentic complex
from human cells. Recombinant human RPA binds single-stranded DNA and is
capable of supporting SV40 DNA replication in vitro. In addition,
recombinant RPA became phosphorylated when incubated under replication
conditions.
Recombinant replication protein A: expression, complex formation, and functional characterization [published erratum appears in J Biol Chem 1994 Jun 10;269(23):16519]
Department of Biochemistry, University of Iowa, Iowa City 52242.
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