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Regulation of mRNA decay in E. coli .

Authors :
Mohanty BK
Kushner SR
Source :
Critical reviews in biochemistry and molecular biology [Crit Rev Biochem Mol Biol] 2022 Feb; Vol. 57 (1), pp. 48-72. Date of Electronic Publication: 2021 Sep 21.
Publication Year :
2022

Abstract

Detailed studies of the Gram-negative model bacterium, Escherichia coli , have demonstrated that post-transcriptional events exert important and possibly greater control over gene regulation than transcription initiation or effective translation. Thus, over the past 30 years, considerable effort has been invested in understanding the pathways of mRNA turnover in E. coli . Although it is assumed that most of the ribonucleases and accessory proteins involved in mRNA decay have been identified, our understanding of the regulation of mRNA decay is still incomplete. Furthermore, the vast majority of the studies on mRNA decay have been conducted on exponentially growing cells. Thus, the mechanism of mRNA decay as currently outlined may not accurately reflect what happens when cells find themselves under a variety of stress conditions, such as, nutrient starvation, changes in pH and temperature, as well as a host of others. While the cellular machinery for degradation is relatively constant over a wide range of conditions, intracellular levels of specific ribonucleases can vary depending on the growth conditions. Substrate competition will also modulate ribonucleolytic activity. Post-transcriptional modifications of transcripts by polyadenylating enzymes may favor a specific ribonuclease activity. Interactions with small regulatory RNAs and RNA binding proteins add additional complexities to mRNA functionality and stability. Since many of the ribonucleases are found at the inner membrane, the physical location of a transcript may help determine its half-life. Here we discuss the properties and role of the enzymes involved in mRNA decay as well as the multiple factors that may affect mRNA decay under various in vivo conditions.

Details

Language :
English
ISSN :
1549-7798
Volume :
57
Issue :
1
Database :
MEDLINE
Journal :
Critical reviews in biochemistry and molecular biology
Publication Type :
Academic Journal
Accession number :
34547957
Full Text :
https://doi.org/10.1080/10409238.2021.1968784