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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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Published in: | The journal of microbiology 2019, 57(10), , pp.910-917 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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
. |
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ISSN: | 1225-8873 1976-3794 |
DOI: | 10.1007/s12275-019-9354-6 |