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J. Bacteriol. doi:10.1128/JB.01243-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Hfq Modulates the ^E-mediated Envelope Stress Response and the ³²-mediated Cytoplasmic Stress Response in Escherichia coli

Departments of Biochemistry and Biophysics, Microbiology and Immunology, and Cell and Tissue Biology, University of California, San Francisco

^* To whom correspondence should be addressed. Email: cgross{at}cgl.ucsf.edu.

	Abstract

Hfq, a chaperone for small non-coding RNAs, regulates many processes in Escherichia coli including the ^S-mediated general stress response. Here, we use microarray analysis to identify the changes in gene expression resulting from lack of Hfq. We identify several potential new targets for Hfq regulation, including genes encoding outer membrane proteins, enzymes, factors and transporters. Many of these genes are involved in amino acid uptake and biosynthesis, sugar uptake and metabolism, and cell energetics. In addition, we find altered regulation of the ^E and ³²-mediated stress responses, which we analyze further. We show that cells lacking Hfq induce the ^E-mediated envelope stress response and are defective in ^E-mediated repression of outer membrane proteins. We also show that the ³²-mediated cytoplasmic stress response is repressed in cells lacking Hfq due to increased expression of DnaK. Furthermore, we show that cells lacking Hfq are defective in "long term adaptation" of ³² to chronic chaperone overexpression. Together, our results indicate that Hfq may play a general role in stress response regulation in E. coli.

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