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(Received for publication, April 4, 1996)
From the Graduate Program in Molecular Biology, Memorial
Sloan-Kettering Cancer Center, New York, New York 10021
We have purified a single-stranded DNA-binding
protein (SSB) from Schizosaccharomyces pombe (Sp) and
have shown that it is composed of three subunits of 68, 30, and 12 kDa.
The SpSSB supports T antigen-dependent unwinding of SV40
ori containing DNA, but is not functional in the SV40
in vitro replication reaction. All three genes that
encode the SpSSB subunit have been isolated. The cloned cDNA of the
ssb1+, encoding the p68 subunit, contains
609 amino acids (68.3 kDa), while that of the
ssb2+, encoding the p30 subunit, contains a
279 amino acids (30.3 kDa). The genomic DNA clone of the p12 subunit
gene (ssb3+) has 2 introns and an open
reading frame of 104 amino acids (11.8 kDa). Significant homology is
observed among the largest and middle subunits of eukaryotic SSBs, but
there is poor homology among the smallest subunits. In addition, we
have reconstituted the SpSSB complex by coexpression of all three
subunits in Escherichia coli. The reconstituted complex
is active in single-stranded DNA binding and the T
antigen-dependent unwinding of SV40 ori DNA.
Finally, we observed a cell cycle-dependent phosphorylation
pattern of the p30 subunit of SpSSB, which is similar to that observed
for the human and Saccharomyces cerevisiae SSB.
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20868-20878
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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