Nucleic Acids Research Advance Access originally published online on July 20, 2009
Nucleic Acids Research 2009 37(16):5477-5485; doi:10.1093/nar/gkp591
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Nucleic Acids Research, 2009, Vol. 37, No. 16 5477-5485
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Characterization of homologs of the small RNA SgrS reveals diversity in function
Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
*To whom correspondence should be addressed. Tel: +1 217 333 7033; Fax: +1 217 244 6697; Email: cvanderp{at}life.illinois.edu
Received April 3, 2009. Revised June 9, 2009. Accepted June 27, 2009.
SgrS is a small RNA (sRNA) that requires the RNA chaperone Hfq for its function. SgrS is a unique dual-function sRNA with a base pairing function that regulates mRNA targets and an mRNA function that allows production of the 43-amino-acid protein SgrT. SgrS is expressed when non-metabolizable sugars accumulate intracellularly (glucose-phosphate stress) and is required to allow Escherichia coli cells to recover from stress. In this study, homologs of SgrS were used to complement an E. coli sgrS mutant in order elucidate the physiological relevance of differences among homologs. These analyses revealed that the base pairing function of E. coli and Yersinia pestis SgrS homologs is critical for rescue from glucose-phosphate stress. In contrast, base pairing-deficient SgrS homologs from Salmonella typhimurium, Erwinia carotovora and Klebsiella pneumoniae rescue E. coli cells from stress despite their failure to regulate target mRNAs. Compared with E. coli SgrS, S. typhimurium SgrS produces more SgrT and this rescues cell growth even when the base pairing function is inactivated. Genetic evidence suggests that a secondary structure in the E. coli SgrS 5' region inhibits sgrT translation. This structure is not present in S. typhimurium SgrS, which explains its higher level of SgrT production.