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Microbiology 150 (2004), 687-695; DOI  10.1099/mic.0.26666-0
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Microbiology 150 (2004), 687-695; DOI  10.1099/mic.0.26666-0
© 2004 Society for General Microbiology

Temperature-dependent processing of the cspA mRNA in Rhodobacter capsulatus

Stephanie Jäger1,{dagger}, Elena Evguenieva-Hackenberg1 and Gabriele Klug1

1 Institut für Mikrobiologie und Molekularbiologie, Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 26, D-35392 Giessen, Germany

Correspondence
Gabriele Klug
Gabriele.Klug{at}mikro.bio.uni-giessen.de

The expression of genes for cold-shock proteins is proposed to be regulated primarily at the post-transcriptional level by increase of mRNA stability after transition to low temperatures. Destabilization of the Escherichia coli cold-induced cspA transcript at 37 °C as well as stabilization upon cold shock is known to depend on the unusually long (159 nt) 5'-untranslated region. Determination of the cspA mRNA 5'-end from Rhodobacter capsulatus revealed a shorter distance between the start of transcription and the start codon for translation. The cspA mRNA of R. capsulatus was shown to be stabilized at low temperatures to a greater extent than other investigated transcripts. To address the mechanism of decay of the cspA transcript, it was incubated with purified degradosome of R. capsulatus. Endoribonucleolytic in vitro cleavage in the 5'-untranslated region as reported for the cspA transcript of E. coli in vivo was not observed. Instead, the data indicated that the cspA mRNA decay in R. capsulatus is mediated by endoribonucleolytic cleavages within the cspA coding region.

Abbreviations: PAA, polyacrylamide; UTR, untranslated region

{dagger}Present address: Institut für Pathologie, Klinikum der Philipps-Universität, Baldingerstraße, D-35043 Marburg, Germany.






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Copyright © 2004 Society for General Microbiology.