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TitleHead swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites.
Journal, issue, pagesNature, Vol. 468, Issue 7324, Page 713-716, Year 2010
Publish dateDec 2, 2010
AuthorsAndreas H Ratje / Justus Loerke / Aleksandra Mikolajka / Matthias Brünner / Peter W Hildebrand / Agata L Starosta / Alexandra Dönhöfer / Sean R Connell / Paola Fucini / Thorsten Mielke / Paul C Whitford / José N Onuchic / Yanan Yu / Karissa Y Sanbonmatsu / Roland K Hartmann / Pawel A Penczek / Daniel N Wilson / Christian M T Spahn /
PubMed AbstractThe elongation cycle of protein synthesis involves the delivery of aminoacyl-transfer RNAs to the aminoacyl-tRNA-binding site (A site) of the ribosome, followed by peptide-bond formation and ...The elongation cycle of protein synthesis involves the delivery of aminoacyl-transfer RNAs to the aminoacyl-tRNA-binding site (A site) of the ribosome, followed by peptide-bond formation and translocation of the tRNAs through the ribosome to reopen the A site. The translocation reaction is catalysed by elongation factor G (EF-G) in a GTP-dependent manner. Despite the availability of structures of various EF-G-ribosome complexes, the precise mechanism by which tRNAs move through the ribosome still remains unclear. Here we use multiparticle cryoelectron microscopy analysis to resolve two previously unseen subpopulations within Thermus thermophilus EF-G-ribosome complexes at subnanometre resolution, one of them with a partly translocated tRNA. Comparison of these substates reveals that translocation of tRNA on the 30S subunit parallels the swivelling of the 30S head and is coupled to unratcheting of the 30S body. Because the tRNA maintains contact with the peptidyl-tRNA-binding site (P site) on the 30S head and simultaneously establishes interaction with the exit site (E site) on the 30S platform, a novel intra-subunit 'pe/E' hybrid state is formed. This state is stabilized by domain IV of EF-G, which interacts with the swivelled 30S-head conformation. These findings provide direct structural and mechanistic insight into the 'missing link' in terms of tRNA intermediates involved in the universally conserved translocation process.
External linksNature / PubMed:21124459 / PubMed Central
MethodsEM (single particle)
Resolution7.6 - 7.8 Å
Structure data

1798

4v5m

EMDB-1798: tRNA translocation on the 70S ribosome: the pre-translocational translocation intermediate TI(PRE)
PDB-4v5m: tRNA tranlocation on the 70S ribosome: the pre-translocational translocation intermediate TI(PRE)
Method: EM (single particle) / Resolution: 7.8 Å

1799

4v5n

EMDB-1799: tRNA translocation on the 70S ribosome: the post-translocational translocation intermediate TI(POST)
PDB-4v5n: tRNA translocation on the 70S ribosome: the post- translocational translocation intermediate TI(POST)
Method: EM (single particle) / Resolution: 7.6 Å

Chemicals

ChemComp-FUA:
FUSIDIC ACID / antibiotic, Antimicrobial*YM / Fusidic acid

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

Source
  • Thermus thermophilus HB8 (bacteria)
  • thermus thermophilus (bacteria)
  • escherichia coli (E. coli)
KeywordsRIBOSOME / TRANSLATION / ELONGATION CYCLE / TRNA TRANSLOCATION

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