The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome

  1. Dmitri Andreev1,
  2. Vasili Hauryliuk2,
  3. Ilya Terenin1,
  4. Sergey Dmitriev1,
  5. Måns Ehrenberg2, and
  6. Ivan Shatsky1
  1. 1Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia
  2. 2Department of Cell and Molecular Biology, BMC, Uppsala University, S-75124 Uppsala, Sweden

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.

Keywords

Footnotes

  • Reprint requests to: Ivan Shatsky, Belozersky Institute of Physico-Chemical Biology, Moscow State University, Building “A,” Moscow 119992, Russia; e-mail: shatsky{at}genebee.msu.su; fax: 7-495-9393181.

  • Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.693208.

    • Received June 20, 2007.
    • Accepted November 7, 2007.
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  1. Published in Advance December 14, 2007, doi: 10.1261/rna.693208 RNA 2008. 14: 233-239 Copyright © 2008 RNA Society

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