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  • Title: Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostrepton.
    Author: Ballesta JP, Vazquez D.
    Journal: Proc Natl Acad Sci U S A; 1972 Oct; 69(10):3058-62. PubMed ID: 4562752.
    Abstract:
    Methanol stimulates the hydrolysis of GTP catalyzed by bacterial ribosomes in the presence of the chain elongation factor T (EF-T). The methanol-stimulated activity is uncoupled from aminoacyl-tRNA binding to the ribosomes and does not require the presence of either synthetic polynucleotide messenger or aminoacyl-tRNA. When these reactants are present, along with EF-T, GTP, and methanol, the ribosomal binding of aminoacyl-tRNA is inhibited by thiostrepton but the uncoupled, EF-T-dependent hydrolysis of GTP is resistant to the antibiotic.
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