title: Elongation factors on the ribosome.
abstract: The ribosome is a complex macromolecular assembly capable of translating mRNA sequence into amino acid sequence. The adaptor molecule of translation is tRNA, but the delivery of aminoacyl-tRNAs--the primary substrate of the ribosome--relies on the formation of a ternary complex with elongation factor Tu (EF-Tu) and GTP. Likewise, elongation factor G (EF-G) is required to reset the elongation cycle through the translocation of tRNAs. Recent structures and biochemical data on ribosomes in complex with the ternary complex or EF-G have shed light on the mode of action of the elongation factors, and how this interplays with the state of tRNAs and the ribosome. A model emerges of the specific routes of conformational changes mediated by tRNA and the ribosome that trigger the GTPase activity of the elongation factors on the ribosome.
authors.affiliation: University of Aarhus, Department of Molecular Biology, Gustav Wieds Vej 10C, 8000 Arhus C, Denmark.
authors.forename: Jakob
authors.initials: J
authors.lastname: Nilsson
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
mesh_terms: D001665:Binding Sites; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D009690:Nucleic Acid Conformation; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D014176:Protein Biosynthesis / Q000502:physiology*; D011487:Protein Conformation; D012343:RNA, Transfer / Q000737:chemistry* / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D013329:Structure-Activity Relationship
chemical_list: D046911:Macromolecular Substances; D010445:Peptide Elongation Factors; D012343:RNA, Transfer