Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostrepton.
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.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002247:Carbon Isotopes; D003864:Depression, Chemical; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000378:metabolism; D005672:Fusidic Acid / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006358:Hot Temperature; D006868:Hydrolysis; D000432:Methanol / Q000494:pharmacology; D009994:Osmolar Concentration; D010445:Peptide Elongation Factors / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D010649:Phenylalanine / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D013268:Stimulation, Chemical
D000900:Anti-Bacterial Agents; D002247:Carbon Isotopes; D010445:Peptide Elongation Factors; D010455:Peptides; D010649:Phenylalanine; D005672:Fusidic Acid; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D000432:Methanol