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Catalysis of ribosomal translocation by sparsomycin | Kurt Fredrick
; Harry F Noller
; | Date: |
16 May 2003 | Journal: | Science, 300 (5622), 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. | Source: | PubMed, pmid12750524 doi: 10.1126/science.1084571 | Services: | Forum | Review | Favorites |
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