Single-molecule analysis of translational dynamics.
Decades of extensive biochemical and biophysical research have outlined the mechanism of translation. Rich structural studies have provided detailed snapshots of the translational machinery at all phases of the translation cycle. However, the relationship between structural dynamics, composition, and function remains unknown. The multistep nature of each stage of the translation cycle results in rapid desynchronization of individual ribosomes, thus hindering elucidation of the underlying mechanisms by conventional bulk biophysical and biochemical methods. Single-molecule approaches unsusceptible to these complications have led to the first glances at both compositional and conformational dynamics on the ribosome and their impact on translational control. These experiments provide the necessary link between static structure and mechanism, often providing new perspectives. Here we review recent advances in the field and their relationship to structural and biochemical data.
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Alexey
A
Petrov
Jin
J
Chen
Seán
S
O'Leary
Albert
A
Tsai
Joseph D
JD
Puglisi
D008957:Models, Genetic; D008967:Molecular Biology / Q000379:methods; D008968:Molecular Conformation; D010441:Peptide Chain Elongation, Translational; D039881:Prokaryotic Initiation Factor-2 / Q000502:physiology; D014176:Protein Biosynthesis / Q000502:physiology*; D012343:RNA, Transfer / Q000502:physiology; D012270:Ribosomes / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure
D039881:Prokaryotic Initiation Factor-2; D012343:RNA, Transfer