The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome |
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Authors: | Andreev Dmitri Hauryliuk Vasili Terenin Ilya Dmitriev Sergey Ehrenberg Måns Shatsky Ivan |
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Institution: | Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. |
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Abstract: | RelE/RelB is a well-characterized toxin-anti-toxin pair involved in nutritional stress responses in Bacteria and Archae. RelE lacks any eukaryote homolog, but we demonstrate here that it efficiently and specifically cleaves mRNA in the A site of the eukaryote ribosome. The cleavage mechanism is similar to that in bacteria, showing the feasibility of A-site cleavage of mRNA for regulatory purposes also in eukaryotes. RelE cleavage in the A-site codon of a stalled eukaryote ribosome is precise and easily monitored, making "RelE printing" a useful complement to toeprinting to determine the exact mRNA location on the eukaryote ribosome and to probe the occupancy of its A site. |
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Keywords: | bacterial toxin RelE eukaryotic ribosomes mRNA cleavage initiation complex assembly toeprinting RelE printing |
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