RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli.
J Microbiol
; 57(10): 910-917, 2019 Oct.
Article
em En
| MEDLINE
| ID: mdl-31571126
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 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.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Triose-Fosfato Isomerase
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RNA Mensageiro
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Proteínas de Escherichia coli
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Endorribonucleases
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Escherichia coli
Idioma:
En
Revista:
J Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2019
Tipo de documento:
Article