Bacterial Toxin RelE Mediates Frequent Codon-independent mRNA Cleavage from the 5′ End of Coding Regions in Vivo

• Published in: The Journal of biological chemistry Vol. 286; no. 17; pp. 14770 - 14778
• Main Authors: Hurley, Jennifer M., Cruz, Jonathan W., Ouyang, Ming, Woychik, Nancy A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.04.2011; American Society for Biochemistry and Molecular Biology
• Subjects: 5' Flanking Region; Antitoxin; Bacteria; Bacterial Toxins - metabolism; Binding Sites; Codon - metabolism; Elongation; Endoribonuclease; Escherichia coli Proteins; Hydrolysis; Protein Biosynthesis; RelB; Ribosomes; RNA; RNA, Messenger - metabolism; Toxins; Translation; Translation; RNA; Ribosomes; Antitoxin; Bacteria; Toxins; Elongation; Endoribonuclease; RelB

The enzymatic activity of the RelE bacterial toxin component of the Escherichia coli RelBE toxin-antitoxin system has been extensively studied in vitro and to a lesser extent in vivo. These earlier reports revealed that 1) RelE alone does not exhibit mRNA cleavage activity, 2) RelE mediates mRNA cle...