title: Insights into the decoding mechanism from recent ribosome structures.
abstract: During the decoding process, tRNA selection by the ribosome is far more accurate than expected from codon-anticodon pairing. Antibiotics such as streptomycin and paromomycin have long been known to increase the error rate of translation, and many mutations that increase or lower accuracy have been characterized. Recent crystal structures show that the specific recognition of base-pairing geometry leads to a closure of the domains of the small subunit around cognate tRNA. This domain closure is likely to trigger subsequent steps in tRNA selection. Many antibiotics and mutations act by making the domain closure more or less favourable. In conjunction with recent cryoelectron microscopy structures of the ribosome, a comprehensive structural understanding of the decoding process is beginning to emerge.
authors.affiliation: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
authors.forename: James M
authors.initials: JM
authors.lastname: Ogle
authors.forename: Andrew P
authors.initials: AP
authors.lastname: Carter
authors.forename: V
authors.initials: V
authors.lastname: Ramakrishnan
mesh_terms: D000926:Anticodon / Q000235:genetics; D001483:Base Sequence; D006160:Guanosine Triphosphate / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000378:metabolism; D014176:Protein Biosynthesis; D017434:Protein Structure, Tertiary; D012345:RNA, Transfer, Amino Acid-Specific / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000926:Anticodon; D012345:RNA, Transfer, Amino Acid-Specific; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu