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• W1888896619 endingPage "117" @default.
• W1888896619 startingPage "111" @default.
• W1888896619 abstract "The functional significance of the post-translocation interaction of eukaryotic ribosomes with EF-2 was studied using the translational inhibitor ricin. Ribosomes treated with ricin showed a decreased rate of elongation accompanied by altered proportions of the different ribosomal phases of the elongation cycle. The content of ribosome-bound EF-2 was diminished by approximately 65% while that of EF-1 was unaffected. The markedly reduced content of EF-2 was caused by an inability of the ricin-treated ribosomes to form high-affinity pre-translocation complexes with EF-2. However, the ribosomes were still able to interact with EF-2 in the form of a low-affinity post-translocation complex. Ricin-treated ribosomes showed an altered ability to stimulate the GTP hydrolysis catalysed by either EF-1 or EF-2. The EF-1-catalysed hydrolysis was reduced by approximately 70%, resulting in a decreased turnover of the quaternary EF-1 X GTP X aminoacyl-tRNA X ribosome complex. In contrast, the EF-2-catalysed hydrolysis was increased by more than 400%, despite the lack of pre-translocation complex formation. The effect was not restricted to empty reconstituted ribosomes since gently salt-washed polysomes also showed an increased rate of GTP hydrolysis. The results indicate that the EF-1- and EF-2-dependent hydrolysis of GTP was activated by a common center on the ribosome that was specifically adapted for promoting the GTP hydrolysis of either EF-1 or EF-2. Furthermore, the results suggest that the GTP hydrolysis catalysed by EF-2 occurred in the low-affinity post-translocation complex." @default.
• W1888896619 created "2016-06-24" @default.
• W1888896619 creator A5027365597 @default.
• W1888896619 creator A5084746931 @default.
• W1888896619 date "1986-11-01" @default.
• W1888896619 modified "2023-10-17" @default.
• W1888896619 title "The mechanism of the protein-synthesis elongation cycle in eukaryotes. Effect of ricin on the ribosomal interaction with elongation factors" @default.
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• W1888896619 doi "https://doi.org/10.1111/j.1432-1033.1986.tb10130.x" @default.
• W1888896619 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3780730" @default.
• W1888896619 hasPublicationYear "1986" @default.
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