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Literature DB >> 4562752

Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostrepton.

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.

Entities: Chemical Disease

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Year: 1972 PMID： 4562752 PMCID： PMC389706 DOI： 10.1073/pnas.69.10.3058

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

22 in total

1. Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes.

Authors: M L. Celma; R E. Monro; D Vazquez
Journal: FEBS Lett Date: 1970-02-16 Impact factor: 4.124

2. The interrelationship between guanosine triphosphatase and amino acid polymerization.

Authors: Y Nishizuka; F Lipmann
Journal: Arch Biochem Biophys Date: 1966-09-26 Impact factor: 4.013

3. Separation of large quantities of ribosomal subunits by zonal ultracentrifugation.

Authors: E F Eikenberry; T A Bickle; R R Traut; C A Price
Journal: Eur J Biochem Date: 1970-01

4. The peptidyl transferase activity of ribosomes.

Authors: R E Monro; T Staehelin; M L Celma; D Vazquez
Journal: Cold Spring Harb Symp Quant Biol Date: 1969

5. Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release.

Authors: R K Tompkins; E M Scolnick; C T Caskey
Journal: Proc Natl Acad Sci U S A Date: 1970-03 Impact factor: 11.205

6. Stoichiometry of aminoacyl-transfer RNA binding and GTP cleavage during chain elongation and translocation.

Authors: Y Ono; A Skoultchi; J Waterson; P Lengyel
Journal: Nature Date: 1969-08-16 Impact factor: 49.962

7. Inhibition by thiopeptin of ribosomal functions associated with T and G factors.

Authors: T Kinoshita; Y Liou; N Tanaka
Journal: Biochem Biophys Res Commun Date: 1971-08-20 Impact factor: 3.575

8. Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol. lincomycin and erythromycin sites.

Authors: R Fernandez-Munoz; R E Monro; R Torres-Pinedo; D Vazquez
Journal: Eur J Biochem Date: 1971-11-11

Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostrepton.

1. Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes.

2. The interrelationship between guanosine triphosphatase and amino acid polymerization.

3. Separation of large quantities of ribosomal subunits by zonal ultracentrifugation.

4. The peptidyl transferase activity of ribosomes.

5. Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release.

6. Stoichiometry of aminoacyl-transfer RNA binding and GTP cleavage during chain elongation and translocation.

7. Inhibition by thiopeptin of ribosomal functions associated with T and G factors.

8. Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol. lincomycin and erythromycin sites.

9. [Determination of orthophosphate in the presence of phosphate compounds with an affinity for acids and molybdate].

10. Inhibition by siomycin and thiostrepton of both aminoacyl-tRNA and factor G binding to ribosomes.

1. An Escherichia coli mutant with an altered elongation factor Tu.

Review 2. Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2.

3. Hydrolysis of GTP on elongation factor Tu.ribosome complexes promoted by 2'(3')-O-L-phenylalanyladenosine.

4. The interaction of elongation factor G with N-acetylphenylalanyl transfer RNA-ribosome complexes.

5. A photoaffinity labelling study of the messenger RNA-binding region of Escherichia coli ribosomes.