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Rapid modulation of RNA function by endoribonucleases during physiological responses to environmental changes is known to be an effective bacterial biochemical adaptation. We report a molecular mechanism underlying the regulation of enolase ( eno ) expression by two endoribonucleases, RNase G and RNase III, the expression levels of which are modulated by oxygen availability in  Escherichia coli . Analyses of transcriptional  eno-cat  fusion constructs strongly suggested the existence of  cis -acting elements in the  eno  5′ untranslated region that respond to RNase III and RNase G cellular concentrations. Primer extension and S1 nuclease mapping analyses of  eno  mRNA  in vivo  identified three  eno  mRNA transcripts that are generated in a manner dependent on RNase III expression, one of which was found to accumulate in  rng -deleted cells. Moreover, our data suggested that RNase III-mediated cleavage of primary  eno  mRNA transcripts enhanced Eno protein production, a process that involved putative  cis -antisense RNA. We found that decreased RNase G protein abundance coincided with enhanced RNase III expression in  E. coli  grown anaerobically, leading to enhanced  eno  expression. Thereby, this posttranscriptional up-regulation of  eno  expression helps  E. coli  cells adjust their physiological reactions to oxygen-deficient metabolic modes. Our results revealed a molecular network of coordinated endoribonuclease activity that post-transcriptionally modulates the expression of Eno, a key enzyme in glycolysis.

The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli