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Updated: May 5, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
Kim Pedersen1, Andrey V Zavialov, Michael Yu Pavlov
1Department of Biochemistry and Molecular Biology, OU, University of Southern Denmark, Campusvej 55, DK-5230 Odense, Denmark.
Abstract:
The Escherichia coli relBE operon encodes a toxin-antitoxin pair, RelE-RelB. RelB can reverse inhibition of protein synthesis by RelE in vivo. We have found that although RelE does not degrade free RNA, it cleaves mRNA in the ribosomal A site with high codon specificity. Among stop codons UAG is cleaved with fast, UAA intermediate and UGA slow rate, while UCG and CAG are cleaved most rapidly among sense codons. We suggest that inhibition of protein synthesis by RelE is reversed with the help of tmRNA, and that RelE plays a regulatory role in bacteria during adaptation to poor growth conditions.
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Types of RNA
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...
Termination of Translation
Leaky Scanning
Coordination of Gene Expression Processes in Bacteria
Translational Regulation
Bacterial Toxins

