PMID:12750524
| Citation |
Fredrick, K and Noller, HF (2003) Catalysis of ribosomal translocation by sparsomycin. Science 300:1159-62 |
|---|---|
| Abstract |
During protein synthesis, transfer RNAs (tRNAs) are translocated from the aminoacyl to peptidyl to exit sites of the ribosome, coupled to the movement of messenger RNA (mRNA), in a reaction catalyzed by elongation factor G (EF-G) and guanosine triphosphate (GTP). Here, we show that the peptidyl transferase inhibitor sparsomycin triggers accurate translocation in vitro in the absence of EF-G and GTP. Our results provide evidence that translocation is a function inherent to the ribosome and that the energy to drive this process is stored in the tRNA-mRNA-ribosome complex after peptide-bond formation. These findings directly implicate the peptidyl transferase center of the 50S subunit in the mechanism of translocation, a process involving large-scale movement of tRNA and mRNA in the 30S subunit, some 70 angstroms away. |
| Links |
PubMed Online version:10.1126/science.1084571 |
| Keywords |
Acylation; Anti-Bacterial Agents/pharmacology; Catalysis; Codon; Enzyme Inhibitors/pharmacology; Escherichia coli; Escherichia coli Proteins/drug effects; Escherichia coli Proteins/metabolism; Peptide Elongation Factor G/metabolism; Peptidyl Transferases/antagonists & inhibitors; Protein Biosynthesis; RNA, Bacterial/drug effects; RNA, Bacterial/metabolism; RNA, Messenger/drug effects; RNA, Messenger/metabolism; RNA, Transfer/drug effects; RNA, Transfer/metabolism; Ribosomes/drug effects; Ribosomes/metabolism; Sparsomycin/pharmacology |
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