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  Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites

Ratje, A. H., Loerke, J., Mikolajka, A., Brunner, M., Hildebrand, P. W., Starosta, A. L., et al. (2010). Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites. Nature, 468(7324), 713-716. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21124459 %> internal-pdf://Ratje-2010-Head swivel on the r-0059591680/Ratje-2010-Head swivel on the r.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-79D7-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-79D8-2
Genre: Journal Article

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Ratje, A. H., Author
Loerke, J., Author
Mikolajka, A., Author
Brunner, M., Author
Hildebrand, P. W., Author
Starosta, A. L., Author
Donhofer, A., Author
Connell, S. R.1, Author              
Fucini, P.2, Author              
Mielke, T.3, Author              
Whitford, P. C., Author
Onuchic, J. N., Author
Yu, Y., Author
Sanbonmatsu, K. Y., Author
Hartmann, R. K., Author
Penczek, P. A., Author
Wilson, D. N.1, Author              
Spahn, C. M.1, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
3Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: Binding Sites; Cryoelectron Microscopy; Crystallography, X-Ray; Guanosine Diphosphate/chemistry/metabolism; Models, Molecular; *Movement; Peptide Elongation Factor G/chemistry/metabolism; Protein Biosynthesis; Protein Conformation; Protein Subunits/chemistry/metabolism; RNA, Transfer/chemistry/*metabolism/ultrastructure; Ribosome Subunits, Small, Bacterial/*chemistry/*metabolism/ultrastructure; Thermus thermophilus/chemistry
 Abstract: 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.

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 Dates: 2010-12-02
 Publication Status: Published in print
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 468 (7324) Sequence Number: - Start / End Page: 713 - 716 Identifier: ISSN: 1476-4687 (Electronic)