Abstract
Studies have shown that many enzymes involved in glycolysis
are upregulated in Escherichia coli endoribonuclease G (rng)
null mutants. However, the molecular mechanisms underlying
the RNase G-associated regulation of glycolysis have
not been characterized. Here, we show that RNase G cleaves
the 5untranslated region of triosephosphate isomerase A
(tpiA) mRNA, leading to destabilization of the mRNA in E.
coli. Nucleotide substitutions within the RNase G cleavage
site in the genome resulted in altered tpiA mRNA stability,
indicating that RNase G activity influences tpiA mRNA
abundance. In addition, we observed that tpiA expression was
enhanced, whereas that of RNase G was decreased, in E. coli
cells grown anaerobically. Our findings suggest that RNase
G negatively regulates tpiA mRNA abundance in response
to oxygen availability in E. coli.
Citations
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