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Journal of Bacteriology, March 2001, p. 1997-2005, Vol. 183, No. 6
Department of Microbiology and Immunology,
Medical College of Ohio, Toledo, Ohio, 43614,1
and Cell Biology and Metabolism Branch, National Institute of
Child Health and Human Development, National Institutes of Health,
Bethesda, Maryland 208922
Received 16 August 2000/Accepted 8 January 2001
DsrA is an 85-nucleotide, untranslated RNA that has multiple
regulatory activities at 30°C. These activities include the
translational regulation of RpoS and H-NS, global transcriptional
regulators in Escherichia coli. Hfq is an E. coli protein necessary for the in vitro and in vivo replication
of the RNA phage Q
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.6.1997-2005.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Hfq Is Necessary for Regulation by the Untranslated
RNA DsrA
and
. Hfq also plays a role in the degradation of
numerous RNA transcripts. Here we show that an hfq mutant
strain is defective for DsrA-mediated regulation of both
rpoS and hns. The defect in rpoS
expression can be partially overcome by overexpression of DsrA. Hfq
does not regulate the transcription of DsrA, and DsrA does not alter the accumulation of Hfq. However, in an hfq mutant,
chromosome-expressed DsrA was unstable (half-life of 1 min) and
truncated at the 3' end. When expressed from a multicopy plasmid, DsrA
was stable in both wild-type and hfq mutant strains, but it
had only partial activity in the hfq mutant strain.
Purified Hfq binds DsrA in vitro. These results suggest that Hfq acts
as a protein cofactor for the regulatory activities of DsrA by either
altering the structure of DsrA or forming an active RNA-protein complex.
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, Medical College of Ohio, 3055 Arlington Ave., Toledo, OH 43614-5806. Phone: (419) 383-5192. Fax: (419) 383-3002. E-mail: dsledjeski{at}mco.edu.
Present address: Bio-Rad Laboratories, Life Science Group,
Hercules, CA 94547.
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