Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis.

ABSTRACT: The regulation of protein synthesis contributes to gene expression in both normal physiology and disease, yet kinetic investigations of the human translation mechanism are currently lacking. Using single-molecule fluorescence imaging methods, we have quantified the nature and timing of structural processes in human ribosomes during single-turnover and processive translation reactions. These measurements reveal that functional complexes exhibit dynamic behaviors and thermodynamic stabilities distinct from those observed for bacterial systems. Structurally defined sub-states of pre- and post-translocation complexes were sensitive to specific inhibitors of the eukaryotic ribosome, demonstrating the utility of this platform to probe drug mechanism. The application of three-color single-molecul

SUBMITTER: Ferguson A 

PROVIDER: S-EPMC4660248 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature