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Temperature-dependent processing of the cspA mRNA in Rhodobacter capsulatus

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 p...

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Published in:Microbiology (Society for General Microbiology) 2004-03, Vol.150 (3), p.687-695
Main Authors: Jager, Stephanie, Evguenieva-Hackenberg, Elena, Klug, Gabriele
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description 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 Present address: Institut für Pathologie, Klinikum der Philipps-Universität, Baldingerstraße, D-35043 Marburg, Germany.
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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. 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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. 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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. 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ispartof Microbiology (Society for General Microbiology), 2004-03, Vol.150 (3), p.687-695
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source Alma/SFX Local Collection
subjects 5' Untranslated Regions
Action of physical and chemical agents on bacteria
Bacterial Proteins - genetics
Bacteriology
Base Sequence
Biological and medical sciences
DNA, Bacterial - genetics
Escherichia coli - genetics
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetics
Microbiology
Rhodobacter capsulatus
Rhodobacter capsulatus - genetics
Rhodobacter capsulatus - metabolism
RNA Processing, Post-Transcriptional
RNA Stability
RNA, Bacterial - genetics
RNA, Bacterial - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Species Specificity
Temperature
Transcription, Genetic
title Temperature-dependent processing of the cspA mRNA in Rhodobacter capsulatus
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