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Journal ArticleDOI

Studies on the role of factor Ts in polypeptide synthesis.

01 Mar 1970-Archives of Biochemistry and Biophysics (Academic Press)-Vol. 137, Iss: 1, pp 262-269
TL;DR: 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'.
Citations
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Journal ArticleDOI
08 Feb 1996-Nature
TL;DR: The crystal structure of the EF- Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å and the interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF -Tu for guanine nucleotides.
Abstract: The crystal structure of the EF-Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dirtier, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.

277 citations

Journal ArticleDOI
TL;DR: It is reported that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins as do molecular chaperones that are involved in protein folding and protein renaturation after stress.

271 citations

Journal ArticleDOI
TL;DR: The polypeptide elongation factors Tu-GDP, Ts and Tu-Ts have been purified from Escherichia coli to homogeneous state as judged by criteria of ultracentrifugation and disc gel electrophoresis.

236 citations

Journal ArticleDOI
TL;DR: Subunit III is shown to be identical to the protein synthesis elongation factor EF Tu by the following criteria: coelectrophoresis on sodium dodecyl sulfate gels, precipitation ofEF Tu by anti-Qbeta replicase serum, binding of guanine nucleotides, and binding of phenylalanyl-tRNA.
Abstract: The enzyme, Qbeta replicase, responsible for the replication of the RNA of Escherichia coli pahge Qbeta, is composed of four nonidentical subunits, three of which, I, III, and IV, are coded for by the bacterial genome, while subunit II is phage-specific. SUBUNIT IV IS SHOWN TO BE IDENTICAL TO THE PROTEIN SYNTHESIS ELONGATION FACTOR EF TS BY THE FOLLOWING CRITERIA: coelectrophoresis on polyacrylamide gels in sodium dodecyl sulfate and in urea buffers, identity of the first seven amino acids at the amino-terminus, precipitation of sub-unit IV by anti-EF T-factor serum, and stimulation of EF Tu-GDP exchange by subunit IV. Subunit III is shown to be identical to the protein synthesis elongation factor EF Tu by the following criteria: coelectrophoresis on sodium dodecyl sulfate gels, precipitation of EF Tu by anti-Qbeta replicase serum, binding of guanine nucleotides, and binding of phenylalanyl-tRNA. In addition, Qbeta replicase activity can be reconstituted from subunits I and II with EF Tu and EF Ts.

224 citations

Journal ArticleDOI
TL;DR: This article aims to overview the recent advances in protein biosynthesis, concentrating on the moonlighting functions of EF-1.
Abstract: Eukaryotic polypeptide elongation factor EF-1 is not only a major translational factor, but also one of the most important multifunctional (moonlighting) proteins. EF-1 consists of four different subunits collectively termed EF-1alphabeta beta'gamma and EF-1alphabeta gammadelta in plants and animals, respectively. EF-1alpha x GTP catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome. EF-1beta beta'gamma (EF-1beta and EF-1beta'), catalyzes GDP/GTP exchange on EF-1alpha x GDP to regenerate EF-1alpha x GTP. EF-1gamma has recently been shown to have glutathione S-transferase activity. EF-2 catalyzes the translocation of peptidyl-tRNA from the A-site to the P-site on the ribosome. Recently, molecular mimicry among tRNA, elongation factors, releasing factor (RF), and ribosome recycling factor (RRF) has been demonstrated and greatly improved our understanding of the mechanism of translation. Moreover, eukaryotic elongation factors have been shown to be concerned or likely to be concerned in various important cellular processes or serious diseases, including translational control, signal transduction, cytoskeletal organization, apoptosis, adult atopic dermatitis, oncogenic transformation, nutrition, and nuclear processes such as RNA synthesis and mitosis. This article aims to overview the recent advances in protein biosynthesis, concentrating on the moonlighting functions of EF-1.

200 citations

References
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Journal ArticleDOI
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.

7,634 citations

Journal ArticleDOI
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.

132 citations

Journal ArticleDOI
17 May 1969-Nature
TL;DR: At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
Abstract: At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.

99 citations

Journal ArticleDOI
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.

98 citations

Journal ArticleDOI
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.

94 citations