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• W2020105636 endingPage "1162" @default.
• W2020105636 startingPage "1159" @default.
• W2020105636 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." @default.
• W2020105636 created "2016-06-24" @default.
• W2020105636 creator A5031416408 @default.
• W2020105636 creator A5089776171 @default.
• W2020105636 date "2003-05-16" @default.
• W2020105636 modified "2023-09-23" @default.
• W2020105636 title "Catalysis of Ribosomal Translocation by Sparsomycin" @default.
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• W2020105636 doi "https://doi.org/10.1126/science.1084571" @default.
• W2020105636 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12750524" @default.
• W2020105636 hasPublicationYear "2003" @default.
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