PMID- 17996252
OWN - NLM
STAT- MEDLINE
DCOM- 20080109
LR  - 20211020
IS  - 1089-8638 (Electronic)
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 374
IP  - 5
DP  - 2007 Dec 14
TI  - Specific interaction between EF-G and RRF and its implication for GTP-dependent 
      ribosome splitting into subunits.
PG  - 1345-58
AB  - After termination of protein synthesis, the bacterial ribosome is split into its 
      30S and 50S subunits by the action of ribosome recycling factor (RRF) and 
      elongation factor G (EF-G) in a guanosine 5'-triphosphate 
      (GTP)-hydrolysis-dependent manner. Based on a previous cryo-electron microscopy 
      study of ribosomal complexes, we have proposed that the binding of EF-G to an 
      RRF-containing posttermination ribosome triggers an interdomain rotation of RRF, 
      which destabilizes two strong intersubunit bridges (B2a and B3) and, ultimately, 
      separates the two subunits. Here, we present a 9-A (Fourier shell correlation 
      cutoff of 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine 
      5'-[(betagamma)-imido]triphosphate x RRF complex and a quasi-atomic model derived 
      from it, showing the interaction between EF-G and RRF on the 50S subunit in the 
      presence of the noncleavable GTP analogue guanosine 
      5'-[(betagamma)-imido]triphosphate. The detailed information in this model and a 
      comparative analysis of EF-G structures in various nucleotide- and ribosome-bound 
      states show how rotation of the RRF head domain may be triggered by various 
      domains of EF-G. For validation of our structural model, all known mutations in 
      EF-G and RRF that relate to ribosome recycling have been taken into account. More 
      importantly, our results indicate a substantial conformational change in the 
      Switch I region of EF-G, suggesting that a conformational signal transduction 
      mechanism, similar to that employed in transfer RNA translocation on the ribosome 
      by EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP 
      hydrolysis, into the domain rotation of RRF that eventually splits the ribosome 
      into subunits.
FAU - Gao, Ning
AU  - Gao N
AD  - Howard Hughes Medical Institute, Wadsworth Center, Empire State Plaza, Albany, NY 
      12201-0509, USA.
FAU - Zavialov, Andrey V
AU  - Zavialov AV
FAU - Ehrenberg, Mans
AU  - Ehrenberg M
FAU - Frank, Joachim
AU  - Frank J
LA  - eng
SI  - PDB/2RDO
GR  - R01 GM029169/GM/NIGMS NIH HHS/United States
GR  - R01 GM070768/GM/NIGMS NIH HHS/United States
GR  - P41 RR001219/RR/NCRR NIH HHS/United States
GR  - R01 GM70768/GM/NIGMS NIH HHS/United States
GR  - R01 GM029169-26/GM/NIGMS NIH HHS/United States
GR  - P41 RR001219-257222/RR/NCRR NIH HHS/United States
GR  - R01 GM055440-08/GM/NIGMS NIH HHS/United States
GR  - R01 GM29169/GM/NIGMS NIH HHS/United States
GR  - P41 RR001219-26/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20071016
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Peptide Elongation Factor G)
RN  - 0 (RNA, Messenger)
RN  - 0 (Ribosomal Proteins)
RN  - 0 (ribosome releasing factor)
RN  - 86-01-1 (Guanosine Triphosphate)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cryoelectron Microscopy
MH  - Guanosine Triphosphate/*metabolism
MH  - Hydrolysis
MH  - Molecular Sequence Data
MH  - Peptide Elongation Factor G/chemistry/*metabolism
MH  - Protein Conformation
MH  - RNA, Messenger/genetics
MH  - Ribosomal Proteins/chemistry/*metabolism
MH  - Ribosomes/*metabolism
MH  - Scattering, Radiation
MH  - Sequence Homology, Amino Acid
PMC - PMC2211570
MID - NIHMS35534
EDAT- 2007/11/13 09:00
MHDA- 2008/01/10 09:00
PMCR- 2008/12/14
CRDT- 2007/11/13 09:00
PHST- 2007/07/16 00:00 [received]
PHST- 2007/09/24 00:00 [revised]
PHST- 2007/10/10 00:00 [accepted]
PHST- 2007/11/13 09:00 [pubmed]
PHST- 2008/01/10 09:00 [medline]
PHST- 2007/11/13 09:00 [entrez]
PHST- 2008/12/14 00:00 [pmc-release]
AID - S0022-2836(07)01344-7 [pii]
AID - 10.1016/j.jmb.2007.10.021 [doi]
PST - ppublish
SO  - J Mol Biol. 2007 Dec 14;374(5):1345-58. doi: 10.1016/j.jmb.2007.10.021. Epub 2007 
      Oct 16.