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J. Biol. Chem., Vol. 277, Issue 17, 14493-14500, April 26, 2002
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From the Department of Biochemistry, The Johns Hopkins University,
Bloomberg School of Public Health, Baltimore, Maryland 21205
The ATP-dependent three-strand
exchange activity of the Streptococcus pneumoniae RecA
protein (RecA(Sp)), like that of the Escherichia coli
RecA protein (RecA(Ec)), is strongly stimulated by the
single-stranded DNA-binding protein (SSB) from either E. coli (SSB(Ec)) or S. pneumoniae (SSB(Sp)). The
RecA(Sp) protein differs from the RecA(Ec) protein, however, in that
its ssDNA-dependent ATP hydrolysis activity is completely
inhibited by SSB(Ec) or SSB(Sp) protein, apparently because these
proteins displace RecA(Sp) protein from ssDNA. These results indicate
that in contrast to the mechanism that has been established for the
RecA(Ec) protein, SSB protein does not stimulate the RecA(Sp)
protein-promoted strand exchange reaction by facilitating the formation
of a presynaptic complex between the RecA(Sp) protein and the ssDNA
substrate. In addition to acting presynaptically, however, it has been
proposed that SSB(Ec) protein also stimulates the RecA(Ec)
protein strand exchange reaction postsynaptically, by binding to the
displaced single strand that is generated when the ssDNA substrate
invades the homologous linear dsDNA. In the RecA(Sp) protein-promoted reaction, the stimulatory effect of SSB protein may be due entirely to
this postsynaptic mechanism. The competing displacement of RecA(Sp)
protein from the ssDNA substrate by SSB protein, however, appears to
limit the efficiency of the strand exchange reaction (especially at
high SSB protein concentrations or when SSB protein is added to the
ssDNA before RecA(Sp) protein) relative to that observed under the same
conditions with the RecA(Ec) protein.
To whom correspondence should be addressed. Tel.: 410-955-3895;
Fax: 410-955-2926; E-mail: fbryant@jhsph.edu.
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