title: Ribosome structure and dynamics during translocation and termination.
abstract: Protein biosynthesis, or translation, occurs on the ribosome, a large RNA-protein assembly universally conserved in all forms of life. Over the last decade, structures of the small and large ribosomal subunits and of the intact ribosome have begun to reveal the molecular details of how the ribosome works. Both cryo-electron microscopy and X-ray crystallography continue to provide fresh insights into the mechanism of translation. In this review, we describe the most recent structural models of the bacterial ribosome that shed light on the movement of messenger RNA and transfer RNA on the ribosome after each peptide bond is formed, a process termed translocation. We also discuss recent structures that reveal the molecular basis for stop codon recognition during translation termination. Finally, we review recent advances in understanding how bacteria handle errors in both translocation and termination.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
authors.forename: Jack A
authors.initials: JA
authors.lastname: Dunkle
authors.forename: Jamie H D
authors.initials: JH
authors.lastname: Cate
mesh_terms: D000818:Animals; D018388:Codon, Terminator; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism; D006801:Humans; D010441:Peptide Chain Elongation, Translational; D010443:Peptide Chain Termination, Translational; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D018388:Codon, Terminator; D012333:RNA, Messenger; D012343:RNA, Transfer; D020963:GTP Phosphohydrolase-Linked Elongation Factors