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RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli

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 5′...

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Bibliographic Details
Published in:The journal of microbiology 2019, 57(10), , pp.910-917
Main Authors: Lee, Jaejin, Lee, Dong-Ho, Jeon, Che Ok, Lee, Kangseok
Format: Article
Language:English
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Summary: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 5′ untranslated 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 .
ISSN:1225-8873
1976-3794
DOI:10.1007/s12275-019-9354-6