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