RecBCD enzyme acts in the major pathway of homologous recombination of
linear DNA in Escherichia coli. The enzyme unwinds DNA and is an ATP-
dependent double-strand and single-strand exonuclease and a single-str
and endonuclease; it acts at Chi recombination hotspots (5'-GCTGGTGG-3
') to produce a recombinogenic single-stranded DNA 3'-end. We found th
at a small RNA with a unique sequence of similar to 24 nt was tightly
bound to RecBCD enzyme and co-purified with it. When added to native e
nzyme this RNA, but not four others, increased DNA unwinding and Chi n
icking activities of the enzyme. In seven similarly active enzyme prep
arations the molar ratio of RNA molecules to RecBCD enzyme molecules r
anged from 0.2 to <0.008. These results suggest that, although this un
ique RNA is not an essential enzyme subunit, it has a biological role
in stimulating RecBCD enzyme activity.