Journal
CELL
Volume 110, Issue 5, Pages 551-561Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(02)00905-4
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In Listeria monocytogenes, virulence genes are maximally expressed at 37degreesC, almost silent at 30degreesC and controlled by PrfA, a transcriptional activator whose expression is thermoregulated. Here, we show that the untranslated mRNA (UTR) preceding prfA, forms a secondary structure, which masks the ribosome binding region. Mutations predicted to destabilize this structure led to virulence gene expression and invasion of mammalian cells at 30degreesC. Chemical probing, native gel electrophoresis, in vitro translation, and compensatory and increased stability mutations demonstrated that the UTR switches between a structure active at high temperatures, and another inactive at low temperatures. Strikingly, when the DNA corresponding to the UTR was fused to gfp in E. coli, bacteria became fluorescent at 37degreesC, but not at 30degreesC. This mechanism of posttranscriptional thermoregulation may have important applications.
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