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Document Version Version Comment Date Status
554591.0 [No comment] 28.03.2011 11:19 Released

ID: 554591.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites
Authors:Ratje, A. H.; Loerke, J.; Mikolajka, A.; Brunner, M.; Hildebrand, P. W.; Starosta, A. L.; Donhofer, A.; Connell, S. R.; Fucini, P.; Mielke, T.; Whitford, P. C.; Onuchic, J. N.; Yu, Y.; Sanbonmatsu, K. Y.; Hartmann, R. K.; Penczek, P. A.; Wilson, D. N.; Spahn, C. M.
Date of Publication (YYYY-MM-DD):2010-12-02
Title of Journal:Nature
Issue / Number:7324
Start Page:713
End Page:716
Review Status:not specified
Audience:Not Specified
Abstract / Description: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.
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
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:%G eng
Identifiers:ISSN:1476-4687 (Electronic) [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [ID No:2]