RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coliopen access
- Authors
- Lee ,Jaejin; Lee, Dong-Ho; Jeon, Che Ok; Lee, Kangseok
- Issue Date
- Oct-2019
- Publisher
- Microbiological Society of Korea
- Keywords
- glycolysis; mRNA abundance; RNase G; rng; tpiA
- Citation
- Journal of Microbiology, v.57, no.10, pp 910 - 917
- Pages
- 8
- Journal Title
- Journal of Microbiology
- Volume
- 57
- Number
- 10
- Start Page
- 910
- End Page
- 917
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/36988
- DOI
- 10.1007/s12275-019-9354-6
- ISSN
- 1225-8873
1976-3794
- 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. © 2019, The Microbiological Society of Korea.
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Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
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