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. 1972 Oct;69(10):3058–3062. doi: 10.1073/pnas.69.10.3058

Elongation Factor T-Dependent Hydrolysis of Guanosine Triphosphate Resistant to Thiostrepton

Juan P G Ballesta 1, David Vazquez 1
PMCID: PMC389706  PMID: 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.

Keywords: ribosomes, E. coli, methanol, GMP-PCH2P, siomycin, fusidic acid

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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