Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chloroplast protein synthesis elongation factor Tu (EF-Tuchl) has been purified to near homogeneity from Euglena gracilis. Chromatography of the postribosomal supernatant of light-induced Euglena on DEAE-Sephadex reveals two forms of EF-Tuchl. Further purification has shown that one species consists of a complex between EF-Tuchl and a factor that stimulates its activity. The other species consists of free EF-TUchl. The factor has been purified from both chromatographic forms by taking advantage of the molecular weight shift that occurs upon disruption of the complex between EF-Tuchl and the stimulatory factor. EF-Tuchl consists of a single polypeptide chain with a molecular weight of about 50,000. EF-Tuchl is as active on Escherichia coli ribosomes as it is on its homologous ribosomes but displays no detectable activity on eukaryotic cytoplasmic ribosomes. It is stimulated in polymerization by E. coli EF-Ts and will form a complex with the prokaryotic factor that can be isolated by gel filtration chromatography. Like E. coli EF-Tu, it is sensitive to modification by N-ethylmaleimide and is inhibited by the antibiotic kirromycin. Thus, the chloroplast factor has many features that reflect the close relationship between prokaryotic and chloroplast translational systems.
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PMID:Euglena gracilis chloroplast elongation factor Tu. Purification and initial characterization. 391 16

The chymotrypsin inhibitor l-1-chloro-4-phenyl-3-toluene-p-sulphonamidobutan-2-one does not inhibit the function of the initiation factor during the formation of the polypeptide chain initiation complex in vitro. Since the inhibitor has been shown previously to inhibit polypeptide chain elongation by reacting with elongation factor EF-Tu, the inhibitor can be used to investigate the initiation and elongation steps of protein biosynthesis separately.
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PMID:Lack of inhibition by L-1-chloro-4-phenyl-3-toluene-p-sulphonamidobutan-2-one (L-1-tosylamido-2-phenylethyl chloromethyl ketone) of the formation of bacterial polypeptide chain initiation complex. 459 Feb 4

We reported elsewhere (Varenne et al., 1982) that, during synthesis of a number of colicins in Escherichia coli, intermediate nascent chains of discrete sizes accumulated, suggesting a variable rate of translation. In this paper, a detailed analysis provides arguments that this phenomenon, at least for the proteins under study, is not related to aspects of messenger RNA such as secondary structure. It is linked to the difference in transfer RNA availability for the various codons. Experimental analysis of translation of other proteins in E. coli confirms that the main origin for the discontinuous translation in the polypeptide elongation cycle is the following. For a given codon, the stochastic search of the cognate ternary complex (aminoacyl-tRNA-EF-Tu-GTP) is the rate-limiting step in the elongation cycle: transpeptidation and translocation steps are much faster. The degree of slackening in ribosome movement is almost proportional to the inverse of tRNA concentrations. The verification of this model and its possible physiological significance are discussed.
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PMID:Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains. 608 18

The coupling with polypeptide synthesis of the ribosome-elongation factor G (EF-G)-dependent GTPase activity was studied in a highly purified system with well characterized NH4Cl-washed ribosomes which were from 55 to 67% active in poly(U)-directed polyphenylalanine synthesis. The lowest stoichiometries of total GTP hydrolysis to polyphenylalanine incorporation (2.4 to 2.8) were observed at concentrations of MgCl2 (4 to 6.5 mM) slightly lower than the Mg2+ optimum for polyphenylalanine synthesis (7 to 8 mM), in a system containing 80 mM NH4Cl or KCl. For minimal stoichiometry, the concentration of EF-G should be rate-limiting, whereas that of EF-T (EF-Tu.EF-Ts) and aminoacyl-tRNA should be in excess, since the coupling of the EF-G GTPase activity depends on ribosomes in pretranslocative state. Under this condition, the apparent Km values for GTP of GTPase activity and polyphenylalanine synthesis are identical, and they are about an order of magnitude lower than the Km of the ribosome-EF-G-dependent GTPase activity uncoupled from polypeptide synthesis. The stoichiometry was calculated without the usual correction fro GTP hydrolysis obtained in the same system lacking elongation factor T or aminoacyl-tRNA. Such a correction causes overestimation of the uncoupled EF-G GTPase activity still present in the complete system, leading to artificially low stoichiometric values.
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PMID:The coupling with polypeptide synthesis of the GTPase activity dependent on elongation factor G. 610 71

The enzymes responsible for replication of the RNA of the single-stranded RNA bacteriophages contain, in addition to one phage-coded polypeptide, three host-coded polypeptides taken from the protein biosynthetic machinery: ribosomal protein S1 and the elongation factors Tu and Ts. While S1 performs a function in RNA replication derived from its protein synthetic function, mRNA binding, the reactions catalysed by the elongation factors in protein synthesis are apparently dispensible for RNA replication. In the replicase, these polypeptides, acting as the EF-Tu . Ts complex, play a fundamental structural role. Replacement of the endogenous EF-Tu with mutant EF-Tu, itself stable, causes the RNA replicase to become unstable. The possibility that EF-Tu . Ts is solely a structural protein in the RNA replicase is suggested by experiments showing that a variety of modifications of the elongation factors can be tolerated without loss of RNA synthetic capacity. In fact, EF-Tu . Ts from distantly related bacterial species can substitute for E. coli EF-Tu . Ts in RNA replicase. Evidence is presented that the high in vitro template specificity of Q beta replicase may be accomplished through modulation of the level of GTP required for initiation of transcription. Different natural and synthetic RNAs require quite different GTP concentrations. Mn2+ ions, which extend the range of templates transcribed by Q beta replicase, lower the requirement for GTP. High ionic strength, which alters the conformation of Q beta replicase such that template specificity is increased, raises the GTP requirement. An additional host coded protein required for in vitro Q beta RNA replication, host factor (HF), interacts specifically with Q beta RNA. This polypeptide acts by allowing Q beta replicase to initiate RNA synthesis with Q beta RNA at reduced GTP concentration.
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PMID:Interaction of host-coded and virus-coded polypeptides in RNA phage replication. 610 96

cDNA as well as amino acid sequencing has revealed the complete primary structure of elongation factor EF-1 alpha from the brine shrimp Artemia. A comparison with the published sequences of bacterial EF-Tu, mitochondrial EF-Tu and chloroplastic EF-Tu shows that distinct areas of these polypeptide chains are conserved in evolution. The evolutionary distance between prokaryotic and eukaryotic types of EF-Tu is larger than among bacterial and organellar EF- Tus . A number of regions present in both EF-Tu and EF-G from Escherichia coli are also found in EF-1 alpha from Artemia.
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PMID:The primary structure of elongation factor EF-1 alpha from the brine shrimp Artemia. 620 45

The effect of streptothricin F on elongation factor-dependent and on elongation factor-free translation systems was studied. Streptothricin F inhibits factor-dependent as well as factor-free polypeptide synthesis. The results suggest that streptothricin F inhibits polypeptide synthesis via interaction with the ribosome. In partial reactions streptothricin F impairs EF-G-dependent translocation and to a lesser extent EF-Tu-dependent binding of aa-RNA to the ribosome, while it does not affect peptide bond formation significantly.
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PMID:Action of streptothricin F on ribosomal functions. 625 35

We purified Q beta replicase containing EF-Ts from Bacillus stearothermophilus in place of the homologous polypeptide from Escherichia coli. The hybrid enzyme was fully active in the transcription of a variety of templates. It was found to be qualitatively similar to native Q beta replicase with respect to a variety of parameters which measure the efficiency of initiation of RNA synthesis. The results demonstrated that Q beta replicase can tolerate substantial alterations in the EF-Tu X Ts component of the enzyme. These alterations resulted in only minor perturbations of catalytic properties.
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PMID:Q beta replicase containing a Bacillus stearothermophilus elongation factor. 633 16

In the course of a structural analysis of the alpha-chain of elongation factor 1 from Artemia salina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli reveals a clear correspondence between the eukaryotic and prokaryotic protein throughout their polypeptide chains. The results support a basic conservation of the structure of the aminoacyl-tRNA carrying enzyme in evolution. The occurrence, in the eukaryotic factor, of several epsilon-trimethyllysine residues, is remarkable.
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PMID:Sequence homology between EF-1 alpha, the alpha-chain of elongation factor 1 from Artemia salina and elongation factor EF-Tu from Escherichia coli. 633 79

The polypeptide elongation factor EF-Tu was isolated from a mitochondrial 100 000 x g supernatant of the yeast Saccharomyces cerevisiae and purified over 880-fold by DEAE-Sephadex chromatography and gel filtration. The factor efficiently replaces bacterial EF-Tu in a phenylalanine polymerizing cell-free system of Escherichia coli, it binds GDP and it protects phenylalanyl-tRNA against hydrolysis of the ester bond in the presence of 10 mM GTP. The polymerizing activity of the mitochondrial factor is inhibited to 90% by 50 microM N-ethylmaleimide and to 50% by 2.5 microM kirromycin. The purified factor contains two major polypeptides of apparent molecular weights 48 000 and 34 000. Antibodies raised against the 48 000-Mr protein react with EF-TuE. coli, as revealed by immune blotting and by the inhibition of phenylalanine polymerization. No reaction was observed between anti-(34 000-Mr) and 48 000-Mr protein or EF-TuE. coli. The 48 000-Mr protein has the same isoelectric point (pI = 6.2) and a content of cysteine and basic amino acids similar to the bacterial EF-Tu. It is concluded that the 48 000-Mr protein is the analogue to EF-TuE. coli, and that yeast mitochondrial EF-Tu is functionally and structurally more related to bacterial EF-Tu than cytosolic EF-1 of the same cell.
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PMID:Mitochondrial polypeptide elongation factor EF-Tu of Saccharomyces cerevisiae. Functional and structural homologies to Escherichia coli EF-Tu. 634 Oct 59


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