title: Structural aspects of translation termination on the ribosome.
abstract: Translation of genetic information encoded in messenger RNAs into polypeptide sequences is carried out by ribosomes in all organisms. When a full protein is synthesized, a stop codon positioned in the ribosomal A site signals termination of translation and protein release. Translation termination depends on class I release factors. Recently, atomic-resolution crystal structures were determined for bacterial 70S ribosome termination complexes bound with release factors RF1 or RF2. In combination with recent biochemical studies, the structures resolve long-standing questions about translation termination. They bring insights into the mechanisms of recognition of all three stop codons, peptidyl-tRNA hydrolysis, and coordination of stop-codon recognition with peptidyl-tRNA hydrolysis. In this review, the structural aspects of these mechanisms are discussed.
authors.affiliation: RNA Therapeutics Institute and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA. andrei.korostelev@umassmed.edu
authors.forename: Andrei A
authors.initials: AA
authors.lastname: Korostelev
mesh_terms: D000818:Animals; D018388:Codon, Terminator / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D010454:Peptide Termination Factors / Q000737:chemistry / Q000378:metabolism; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*
chemical_list: D018388:Codon, Terminator; D010454:Peptide Termination Factors; D012346:RNA, Transfer, Amino Acyl; C019037:tRNA, peptidyl-