Relaxed Cleavage Specificity within the RelE Toxin Family
نویسندگان
چکیده
منابع مشابه
The Bacterial Toxin RelE Displays Codon-Specific Cleavage of mRNAs in the Ribosomal A Site
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 am...
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متن کاملThe Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE
Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 A) and bound to progra...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2013
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.02266-12