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Journal of Bacteriology, June 2007, p. 4353-4358, Vol. 189, No. 12
0021-9193/07/$08.00+0 doi:10.1128/JB.00193-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Department of Biochemistry and Molecular Biology, University of British Columbia, Life Sciences Centre, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada V6T 1Z3
Received 5 February 2007/ Accepted 30 March 2007
Degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30°C and is moderately dependent on RNase E. Investigations in vitro show that degradosomes prepared from normal or cold-shocked cultures cleave the cspA mRNA preferentially at a single site in vitro between two stem-loops
24 residues 3' to the termination codon and
31 residues from the 3' end. The site of cleavage is independent of the temperature and largely independent of the phosphorylation status of the 5' end of cspA mRNA. A 5' stem-loop, potential occlusion of the initiation and termination codons, temperature-dependent translational efficiency, and the position of the RNase E cleavage site can explain the differential stability of the cspA mRNA.
Published ahead of print on 6 April 2007.
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