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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.
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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'.

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Citations
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Journal ArticleDOI

Preparation of nucleotide-free elongation factor Tu and its stabilization by the antibiotic kirromycin.

TL;DR: A rapid, highly reproducible procedure for the preparation of nucleotide-free elongation factor Tu (EF-Tu) is described, which takes less than 30 min and allows the prepared of nanomole amounts of the factor.
Journal ArticleDOI

Conformational Transition in Polypeptide Elongation Factor Tu as Revealed by Electron Spin Resonance

TL;DR: The spectral changes unequivocally demonstrate that a reversible conformational change does occur in EF-Tu near the active site induced by the ligand conversion from GDP to GTP.
Journal ArticleDOI

Guanylate cyclase in Escherichia coli. Purification and properties.

TL;DR: Guanylate cyclase has been purified from extracts of Escherichia coli and disc gel electrophoretic analysis indicates that the enzyme consists of a single polypeptide chain, which is distinct from adenylate cyclase.
Journal ArticleDOI

Irreversible inhibition of the interaction between elongation factor Tu and phenylalanyl transfer ribonucleic acid by L-1-tosylamido-2-phenylethyl chloromethy ketone.

TL;DR: The present evidence is consistent with the view that TPCK inactivates EF-Tu by specifically reacting with some portion of the site of phenylalanyl-tRNA binding, which is a known intermediate in its transfer to the ribosome.
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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
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