Journal ArticleDOI
Studies on the role of factor Ts in polypeptide synthesis.
TLDR
The possibility is discussed that Ts is required to dissociate the Tu-GDP complex formed during the binding of AA-tRNA to ribosomes.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1970-03-01. It has received 108 citations till now. The article focuses on the topics: GTP'.read more
Citations
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Journal ArticleDOI
Aminoacyl-tRNA-Tu-GTP interaction with ribosomes
TL;DR: Under the conditions used in the present study, it was possible to show that during the interaction of the ternary complex with the 70S ribosome, the rate of release of Tu-GDP from the complex was faster than the formation of a stable Phe-tRNA mesenger-ribosome complex.
Journal ArticleDOI
Interaction of brain transferase I with guanosine nucleotides and aminoacyl-tRNA.
Hong-Mo Moon,Herbert Weissbach +1 more
TL;DR: The data suggest that a transferase I-GTP complex can be formed which interacts with aminoacyl-tRNA to yield an aminoacyL-t RNA-transferase I -GTPcomplex.
Journal ArticleDOI
Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex
Benjamin J. Burnett,Roger B. Altman,Ryan Ferrao,Jose L. Alejo,Navdep Kaur,Joshua Kanji,Scott C. Blanchard +6 more
TL;DR: In this article, the authors quantitatively explore the kinetic features of Escherichia coli ternary complex formation and decay and suggest that both processes are controlled by a nucleotide-dependent, rate-determining conformational change in elongation factor Tu (EF-Tu) and GTP.
Journal ArticleDOI
The effect of guanosine nucleotides on the multiple forms of protein synthesis elongation factor 1 from wheat embryos
Adela Tarragó,Adela Tarragó,Jorge E. Allende,Jorge E. Allende,Betty Redfield,Betty Redfield,Herbert Weissbach,Herbert Weissbach +7 more
TL;DR: Two species of elongation factor 1 from wheat embryo have been detected by sucrose gradient analysis and Sephadex gel filtration and Aminoacyl-tRNA which reacts preferentially with EF1 l favors the conversion of EF1 h toEF1 l with GTP.
Journal ArticleDOI
Formation of a ternary complex between formylatable yeast Met-tRNA, GTP and binding factor T of yeast and of E. coli.
Dietmar Richter,Fritz Lipmann +1 more
TL;DR: Both formylatable and non-formylatable met-tRNAs of yeast bind to the elongation factor T which transfers aminoacyl-tRNA to the ribosome, which means that yeast cannot use the same mechanism as E. coli for distinguishing initiator tRNA from other aminoacyL tRNAs.
References
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Journal ArticleDOI
A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter
TL;DR: A modification of the naphthalene-dioxane-PPO liquid scintillator has been described which will allow up to 3.0 ml of an aqueous solution to be counted as mentioned in this paper.
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Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes
TL;DR: It is concluded that, although GTP hydrolysis resulted from the binding of aminoacyl-tRNA to ribosomes in a 1:1 stoichiometry, the two reactions were not tightly coupled under all experimental conditions.
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Peptide Chain Elongation: GTP Cleavage catalysed by Factors binding Aminoacyl-Transfer RNA to the Ribosome
TL;DR: At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
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Evidence for a guanine nucleotide-aminoacyl-RNA complex as an intermediate in the enzymatic transfer of aminoacyl-RNA to ribosomes
TL;DR: Preliminary data indicate that F-I catalyzes the formation of a guanine nucleotide-aminoacyl-RNA complex which may be the intermediate product formed in the “enzymatic” transfer of aminoacyL-RNA to ribosomes.
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Formation and properties of the aminoacyl transfer ribonucleic acid-guanosine triphosphate-protein complex.
TL;DR: Evidence is provided that the aminoacyl-tRNA-GTP-FIu complex is an intermediate in the GTP-dependent binding of aminoacy-tRNAs to ribosomes, which is inhibited by chlortetracycline but not by deacylated tRNA.