| 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. |