Title |
RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli |
Author |
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon*, and Kangseok Lee* |
Address |
Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea |
Bibliography |
Journal of Microbiology, 57(10),910–917, 2019,
|
DOI |
10.1007/s12275-019-9354-6
|
Key Words |
glycolysis, mRNA abundance, rng, RNase G, tpiA |
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. |