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Vol. 13, No. 7, pp. 901-911, April 1, 1999
, resulting in constitutive recombination activation
1 Biochemistry and Molecular Biology Graduate Group,
2 Genetics Graduate Group, 3 Sections of
Microbiology and Molecular and Cellular Biology, University of
California, Davis, California 95616-8665 USA
Double-strand DNA break repair and homologous recombination in
Escherichia coli proceed by the RecBCD pathway, which is
regulated by cis-acting elements known as 
sites. A
crucial feature of this regulation is the RecBCD enzyme-directed
loading of RecA protein specifically onto the 3'-terminal,
-containing DNA strand. Here we show that RecBC enzyme (lacking the
RecD subunit) loads RecA protein constitutively onto the
3'-terminal DNA strand, with no requirement for . This strand is
preferentially utilized in homologous pairing reactions. We propose
that RecA protein loading is a latent property of the RecBCD
holoenzyme, which is normally blocked by the RecD subunit and is
revealed following interaction with .
[Key Words:
RecBC; RecA; helicase; ; recombination; DNA repair]
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