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Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic

Hirokawa, G; Kiel, MC; Muto, A; Selmer, Maria LU ; Raj, VS; Liljas, Anders LU ; Igarashi, K; Kaji, H and Kaji, A (2002) In EMBO Journal 21(9). p.2272-2281
Abstract
Ribosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal complex. Inhibitors of translocation, thiostrepton, viomycin and aminoglycosides, inhibited the release of tRNA and mRNA from the post-termination complex. In contrast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translocation, inhibited mRNA but not tRNA release from the complex. The release of tRNA is a prerequisite for mRNA release but partially takes place with EF-G alone. The data are consistent with the notion that RRF binds to the A-site and is translocated to the P-site, releasing deacylated tRNA from the P- and E-sites. The final step, the release of mRNA, is accompanied... (More)
Ribosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal complex. Inhibitors of translocation, thiostrepton, viomycin and aminoglycosides, inhibited the release of tRNA and mRNA from the post-termination complex. In contrast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translocation, inhibited mRNA but not tRNA release from the complex. The release of tRNA is a prerequisite for mRNA release but partially takes place with EF-G alone. The data are consistent with the notion that RRF binds to the A-site and is translocated to the P-site, releasing deacylated tRNA from the P- and E-sites. The final step, the release of mRNA, is accompanied by the release of RRF and EF-G from the ribosome. With the model post-termination complex, 70S ribosomes were released from the post-termination complex by the RRF reaction and were then dissociated into subunits by IF3. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
RRF, protein synthesis, antibiotics, elongation factor G, translocation
in
EMBO Journal
volume
21
issue
9
pages
2272 - 2281
publisher
Oxford University Press
external identifiers
  • wos:000175393700023
  • pmid:11980724
  • scopus:0036566330
ISSN
1460-2075
DOI
10.1093/emboj/21.9.2272
language
English
LU publication?
yes
id
e7343059-9f22-4046-ae53-797584be6ac6 (old id 338667)
date added to LUP
2007-10-22 09:03:29
date last changed
2017-11-19 04:04:44
@article{e7343059-9f22-4046-ae53-797584be6ac6,
  abstract     = {Ribosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal complex. Inhibitors of translocation, thiostrepton, viomycin and aminoglycosides, inhibited the release of tRNA and mRNA from the post-termination complex. In contrast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translocation, inhibited mRNA but not tRNA release from the complex. The release of tRNA is a prerequisite for mRNA release but partially takes place with EF-G alone. The data are consistent with the notion that RRF binds to the A-site and is translocated to the P-site, releasing deacylated tRNA from the P- and E-sites. The final step, the release of mRNA, is accompanied by the release of RRF and EF-G from the ribosome. With the model post-termination complex, 70S ribosomes were released from the post-termination complex by the RRF reaction and were then dissociated into subunits by IF3.},
  author       = {Hirokawa, G and Kiel, MC and Muto, A and Selmer, Maria and Raj, VS and Liljas, Anders and Igarashi, K and Kaji, H and Kaji, A},
  issn         = {1460-2075},
  keyword      = {RRF,protein synthesis,antibiotics,elongation factor G,translocation},
  language     = {eng},
  number       = {9},
  pages        = {2272--2281},
  publisher    = {Oxford University Press},
  series       = {EMBO Journal},
  title        = {Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic},
  url          = {http://dx.doi.org/10.1093/emboj/21.9.2272},
  volume       = {21},
  year         = {2002},
}