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

Andreev, Dmitri ; Hauryliuk, Vasili LU orcid ; Terenin, Ilya ; Dmitriev, Sergey ; Ehrenberg, Måns and Shatsky, Ivan (2008) In RNA 14(2). p.233-239
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. Published by Cold Spring Harbor Laboratory Press.

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author
; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bacterial toxin RelE, Eukaryotic ribosomes, Initiation complex assembly, mRNA cleavage, RelE printing, Toeprinting
in
RNA
volume
14
issue
2
pages
233 - 239
publisher
Cold Spring Harbor Laboratory Press (CSHL)
external identifiers
  • scopus:38649111610
  • pmid:18083838
ISSN
1355-8382
DOI
10.1261/rna.693208
language
English
LU publication?
no
additional info
Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
id
715075fe-29a3-4970-aa20-f78c724147f2
date added to LUP
2021-09-24 20:51:38
date last changed
2024-05-04 13:51:56
@article{715075fe-29a3-4970-aa20-f78c724147f2,
  abstract     = {{<p>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. Published by Cold Spring Harbor Laboratory Press.</p>}},
  author       = {{Andreev, Dmitri and Hauryliuk, Vasili and Terenin, Ilya and Dmitriev, Sergey and Ehrenberg, Måns and Shatsky, Ivan}},
  issn         = {{1355-8382}},
  keywords     = {{Bacterial toxin RelE; Eukaryotic ribosomes; Initiation complex assembly; mRNA cleavage; RelE printing; Toeprinting}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{233--239}},
  publisher    = {{Cold Spring Harbor Laboratory Press (CSHL)}},
  series       = {{RNA}},
  title        = {{The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome}},
  url          = {{http://dx.doi.org/10.1261/rna.693208}},
  doi          = {{10.1261/rna.693208}},
  volume       = {{14}},
  year         = {{2008}},
}