Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G
Zavialov, Andrey V. ; Hauryliuk, Vasili V. LU
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)
- author
- Zavialov, Andrey V.
; Hauryliuk, Vasili V.
LU
and Ehrenberg, Måns
- publishing date
- 2005-06-10
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Cell
- volume
- 18
- issue
- 6
- pages
- 675 - 686
- publisher
- Cell Press
- external identifiers
-
- scopus:20444420154
- pmid:15949442
- 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
- 2026-01-13 21:33:35
@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}},
}