RraA is a protein inhibitor of RNase E, which degrades and
processes numerous RNAs in Escherichia coli. Streptomyces
coelicolor also contains homologs of RNase E and RraA,
RNase ES and RraAS1/RraAS2, respectively. Here, we report
that, unlike other RraA homologs, RraAS1 directly interacts
with the catalytic domain of RNase ES to exert its inhibitory
effect. We further show that rraAS1 gene deletion in S. coelicolor
results
in a higher growth rate and increased production
of actinorhodin and undecylprodigiosin, compared with
the wild-type strain, suggesting that RraAS1-mediated regulation
of RNase ES activity contributes to modulating the
cellular physiology of S. coelicolor.