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J Biol Chem, Vol. 274, Issue 38, 27139-27144, September 17, 1999
From the Sections of Microbiology and of Molecular and Cellular
Biology, University of California, Davis, California 95616-8665
Homologous recombination and double-stranded DNA
break repair in Escherichia coli are initiated by the
multifunctional RecBCD enzyme. After binding to a double-stranded DNA
end, the RecBCD enzyme unwinds and degrades the DNA processively. This
processing is regulated by the recombination hot spot, Chi (
:
5'-GCTGGTGG-3'), which induces a switch in the polarity of DNA
degradation and activates RecBCD enzyme to coordinate the loading
of the DNA strand exchange protein, RecA, onto the single-stranded
DNA products of unwinding. Recently, a single mutation in RecB,
Asp-1080 
Ala, was shown to create an enzyme
(RecBD1080ACD) that is a processive helicase but not a
nuclease. Here we show that the RecBD1080ACD enzyme is also
unable to coordinate the loading of the RecA protein, regardless of
whether sites are present in the DNA. However, the
RecBD1080ACD enzyme does respond to sites by
inactivating in a -dependent manner. These data define a
locus of the RecBCD enzyme that is essential not only for nuclease
function but also for the coordination of RecA protein loading.
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