期刊
MOLECULAR CELL
卷 60, 期 3, 页码 475-486出版社
CELL PRESS
DOI: 10.1016/j.molcel.2015.09.013
关键词
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资金
- NIH [GM 079238]
- Tri-Institutional Stem Cell Initiative - Starr Foundation
- Tri-Institutional Training Program in Chemical Biology
- German Academic Exchange Service
- Swedish Research Council
- VINNMER-Marie Curie International Qualification
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-molecule fluorescence resonance energy transfer (smFRET) methods further revealed a long-distance allosteric coupling between distal tRNA binding sites within ribosomes bearing three tRNAs, which contributed to the rate of processive translation.
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