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

RNA. 2008 Feb;14(2):233-9. doi: 10.1261/rna.693208. Epub 2007 Dec 14.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Toxins / chemistry*
  • Base Sequence
  • Escherichia coli Proteins / chemistry*
  • Genetic Techniques
  • Hepacivirus / genetics
  • Protein Biosynthesis
  • RNA, Messenger / chemistry*
  • RNA, Transfer / chemistry
  • RNA, Viral / chemistry
  • Rabbits
  • Reticulocytes / chemistry
  • Ribosomes / chemistry*


  • Bacterial Toxins
  • Escherichia coli Proteins
  • RNA, Messenger
  • RNA, Viral
  • RelE protein, E coli
  • RNA, Transfer