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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

The mechanism of action of initiation factor F1 from Escherichia coli

TL;DR: Evidence is presented that F1 mediates the recycling of initiation factor F2, a process which needs hydrolysis of GTP, and a stoichiometric system is converted into a catalytic system.
Journal ArticleDOI

Gram‐Scale Purification of Methionyl‐tRNA and Tyrosyl‐tRNA Synthetases from Escherichia coli

TL;DR: The procedure permits the isolation of many enzymes simultaneously and the elution positions of seven other aminoacyl-tRNA synthetases, catalase, rhodanese, phosphofructokinase, elongation factor Tu and cytochrome b-562 are indicated.
Journal ArticleDOI

Characterization of regular polymerization products of elongation factor EF-Tu from Escherichia coli by electron microscopy and image processing

TL;DR: The present study illustrates that the multi-functional protein EF-Tu, which can undergo various allosteric transitions, can assemble into different supramolecular structures.
Journal ArticleDOI

Direct evidence of an elongation factor-Tu/Ts·GTP·Aminoacyl-tRNA quaternary complex.

TL;DR: The generality of this newly described EF-Ts function is revealed and the first direct evidence of the transient quaternary complex species is shown, suggesting thatEF-Ts may regulate ternary complex abundance in the cell through mechanisms that are distinct from its guanosine nucleotide exchange factor functions.
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.
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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