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

Autor: Min-Ho Lee, Ji-Hyun Yeom, Hyun-Lee Kim, Nam-Chul Ha, Jaejin Lee, Se-Hoon Sim, Minkyung Ryu, Minji Sim, Minju Joo, Kangseok Lee, Jang-Cheon Cho, Yoonsoo Hahn
Rok vydání: 2019
Předmět:
Zdroj: Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)
ISSN: 2045-2322
DOI: 10.1038/s41598-019-53883-y
Popis: 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.
Databáze: OpenAIRE