The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli.
Sci Rep
; 9(1): 17257, 2019 11 21.
Article
em En
| MEDLINE
| ID: mdl-31754158
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Fosfopiruvato Hidratase
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Proteínas de Escherichia coli
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Ribonuclease III
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Endorribonucleases
Idioma:
En
Revista:
Sci Rep
Ano de publicação:
2019
Tipo de documento:
Article