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
Function and Structure in Ribonucleic Acid Phage Qβ Ribonucleic Acid Replicase: THE ROLES OF THE DIFFERENT SUBUNITS IN TRANSCRIPTION OF SYNTHETIC TEMPLATES
TL;DR: The role of EF-T in the initiation of RNA synthesis on synthetic templates is not simply related to the functions it performs in protein biosynthesis, but appears to play an essential role in maintaining the active conformation of the replicase enzyme complex.
Journal ArticleDOI
Purification of various forms of elongation factor 1 from rabbit reticulocytes
TL;DR: Using the conventional methods of gel-filtration and ion-exchange chromatography, various forms of elongation factor 1 have been purified from rabbit reticulocyte lysate and it is concluded that EF-1 delta is probably a breakdown product ofEF-1 gamma, and that the native form of EF- 1H probably contains only the alpha, beta, and gamma subunits.
Journal ArticleDOI
Isolation and functional analysis of histidine-tagged elongation factor Tu.
TL;DR: In-vitro and in-vivo functional analyses show thatEF-TuHis resembles the wild-type EF-Tu, which makes this one-step isolation procedure a promising tool for the study of the interactions of mutant EF- Tu with the various components of the elongation cycle.
Journal ArticleDOI
Protection of ribosomes from thiostrepton inactivation by the binding of G factor and guanosine diphosphate.
Journal ArticleDOI
Purification of factor Ts: studies on the formation and stability of nucleotide complexes containing transfer factor Tu.
TL;DR: Transfer factor Ts has been purified to near homogeneity from E. coli and it has been used in studies on the ionic requirements for Tu-nucleotide interaction and Mg 2+ has been shown to have a stabilizing effect on theTu-GDP and Tu-GTP complexes.
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.
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.