Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G

Zavialov, Andrey V. ; Hauryliuk, Vasili V. LU orcid and Ehrenberg, Måns (2005) In Molecular Cell 18(6). p.675-686
Abstract

After peptide release by a class-1 release factor, the ribosomal subunits must be recycled back to initiation. We have demonstrated that the distance between a strong Shine-Dalgarno (SD) sequence and a codon in the P site is crucial for the binding stability of the deacylated tRNA in the P site of the posttermination ribosome and the in-frame maintenance of its mRNA. We show that the elongation factor EF-G and the ribosomal recycling factor RRF split the ribosome into subunits in the absence of initiation factor 3 (IF3) by a mechanism that requires both GTP and GTP hydrolysis. Taking into account that EF-G in the GTP form and RRF bind with positive cooperativity to the free 50S subunit but with negative cooperativity to the 70S... (More)

After peptide release by a class-1 release factor, the ribosomal subunits must be recycled back to initiation. We have demonstrated that the distance between a strong Shine-Dalgarno (SD) sequence and a codon in the P site is crucial for the binding stability of the deacylated tRNA in the P site of the posttermination ribosome and the in-frame maintenance of its mRNA. We show that the elongation factor EF-G and the ribosomal recycling factor RRF split the ribosome into subunits in the absence of initiation factor 3 (IF3) by a mechanism that requires both GTP and GTP hydrolysis. Taking into account that EF-G in the GTP form and RRF bind with positive cooperativity to the free 50S subunit but with negative cooperativity to the 70S ribosome, we suggest a mechanism for ribosome recycling that specifies distinct roles for EF-G, RRF, and IF3.

(Less)
Please use this url to cite or link to this publication:
author
; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Cell
volume
18
issue
6
pages
675 - 686
publisher
Cell Press
external identifiers
  • pmid:15949442
  • scopus:20444420154
ISSN
1097-2765
DOI
10.1016/j.molcel.2005.05.016
language
English
LU publication?
no
additional info
Funding Information: This work was supported by grants from the Swedish Research Council. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
id
57746f40-128a-40d4-a0f8-291741f6feb3
date added to LUP
2021-09-24 20:54:23
date last changed
2024-06-15 18:00:51
@article{57746f40-128a-40d4-a0f8-291741f6feb3,
  abstract     = {{<p>After peptide release by a class-1 release factor, the ribosomal subunits must be recycled back to initiation. We have demonstrated that the distance between a strong Shine-Dalgarno (SD) sequence and a codon in the P site is crucial for the binding stability of the deacylated tRNA in the P site of the posttermination ribosome and the in-frame maintenance of its mRNA. We show that the elongation factor EF-G and the ribosomal recycling factor RRF split the ribosome into subunits in the absence of initiation factor 3 (IF3) by a mechanism that requires both GTP and GTP hydrolysis. Taking into account that EF-G in the GTP form and RRF bind with positive cooperativity to the free 50S subunit but with negative cooperativity to the 70S ribosome, we suggest a mechanism for ribosome recycling that specifies distinct roles for EF-G, RRF, and IF3.</p>}},
  author       = {{Zavialov, Andrey V. and Hauryliuk, Vasili V. and Ehrenberg, Måns}},
  issn         = {{1097-2765}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{6}},
  pages        = {{675--686}},
  publisher    = {{Cell Press}},
  series       = {{Molecular Cell}},
  title        = {{Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G}},
  url          = {{http://dx.doi.org/10.1016/j.molcel.2005.05.016}},
  doi          = {{10.1016/j.molcel.2005.05.016}},
  volume       = {{18}},
  year         = {{2005}},
}