Stability of the osmoregulated promoter-derived proP mRNA is posttranscriptionally regulated by RNase III in Escherichia coli.

ABSTRACT:

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The enzymatic activity of Escherichia coli endo-RNase III determines the stability of a subgroup of mRNA species, including bdm, betT, and proU, whose protein products are associated with the cellular response to osmotic stress. Here, we report that the stability of proP mRNA, which encodes a transporter of osmoprotectants, is controlled by RNase III in response to osmotic stress. We observed that steady-state levels of proP mRNA and ProP protein are inversely correlated with cellular RNase III activity and, in turn, affect the proline uptake capacity of the cell. In vitro and in vivo analyses of proP mRNA revealed RNase III cleavage sites in a stem-loop within the 5' untranslated region present only in proP mRNA species synthesized from the osmoregulated P1 promoter. In

SUBMITTER: Lim B 

PROVIDER: S-EPMC4352664 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature