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Results for “Tryptophan-tRNA Ligase”

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At least 19 recordsLinked to original sources
PubMed1977

Aminoacylation of tRNA Trp from beef liver, yeast and E. coli by beef pancrease tryptophan-tRNA ligase. Stoichiometry of tRNATrp binding.

The Michaelis constants and the maximum velocities in the aminoacylation reaction of tRNATrp from beef liver, yeast and E. coli by pure beef pancreas tryptophan-tRNA ligase show that this mammalian enzyme recognizes and charges the two eucaryotic tRNAs with the same efficiency. The rate of aminoacylation of the procaryotic tRNATrp by the enzyme is three orders of magnitude lower. The pH optimum of aminoacylation is 8 for both eucaryotic tRNAs. The optimum magnesium concentration is different. The rate is maximum when magnesium concentration is stoichiometric to ATP concentration for tRNATrp from beef liver and 10 mM above ATP concentration for tRNATrp from yeast. The number of binding sites on the enzyme for the two eucaryotic tRNAs has been measured by equilibrium filtration on Sephadex G-100 and found equal to two.

Adenosine Triphosphate↗
PubMed1975

The plant aminoacyl-tRNA synthetases. Purification and characterization of valyl-tRNA, tryptophanyl-tRNA and seryl-tRNA synthetases from yellow-lupin seeds.

Valyl-tRNA, tryptophanyl-tRNA, and seryl-tRNA synthetases from yellow lupin seeds Lupinus luteus were purified to homogeneity by ammonium sulfate fractionation, hydrophobic chromatography on aminohexyl-Sepharose column and affinity chromatography on tRNA-Sepharose column. Valyl-tRNA synthetase consists of one polypeptide chain of molecular weight 125000 as judged by Sephadex G-200 gel filtration and dodecylsulfate-polyacrylamide gel electrophoresis in the presence of reducing agent. Seryl-tRNA synthetase, Mr equals 110000, is composed of two 55000-Mr subunits. Tryptophanyl-tRNA synthetase exhibits molecular weight of 200000 on Sephadex G-200 and 37000 in dodecylsulfate-polyacrylamide gel electrophoresis. This indicates that tryptophanyl-tRNA synthetase consists of several subunits (probably four). Since the seryl-tRNA synthetase exhibits the same mobility on dodecylsulfate-polyacrylamide gels both in the presence and absence of reducing agent it is concluded that there is no covalent bond(s) between the subunits of the enzyme. There is also no covalent bond(s) between the subunits of tryptophanyl-tRNA synthetase. Effect of anti-sulfhydryl reagents, monovalent salts, pH and different buffers on activity of the three synthetases is described. Kinetic constants for the substrates of the synthetases are also given. dATP is a substrate for seryl-tRNA synthetase but not for valyl-tRNA and tryptophanyl-tRNA synthetases.

Amino Acyl-tRNA Synthetases↗
PubMed1976

A transcriptional barrier in the regulatory region of the tryptophan operon of Escherichia coli: its role in the regulation of repressor-independent RNA synthesis.

A study was made of the influence of the growth rate of Escherichia coli bacteria on the transcription of the tryptophan (trp) operon, in various trp repressor negative strains. Selective measurement of the levels of RNA transcribed from the regulatory region (reg) of this operon and from the structural genes, respectively, has revealed that the increase of the rate of trpRNA synthesis with bacterial growth rate (Rose and Yanofsky, 1972) is due to a decrease of the frequency of termination of transcription at the transcriptional barrier in the regulatory region of the operon. In a mutant strain of E. coli with a deletion covering the promotor distal part of the regulatory region of the trp operon where the barrier is located, the rate of trpRNA synthesis is not affected by the growth rate. In suA- strains, in which Rho factor activity is reduced the bacterial growth rate does not affect the rate of synthesis of trpRNA. This result suggests that in wild type bacteria Rho factor contributes to the control of the transcription of the trp operon. In bacteria with a mutation rendering Tryptophanyl-tRNA synthetase (TRSase) inactive (trpS- strains) the rate of trpRNA synthesis is affected by the growth rate in the same way as in the isogenic wild type bacteria. This result indicates that TRSase plays no obligatory role in the control of trpRNA synthesis through a mechanism of termination and anti-termination of transcription, at least not in the studied strains, which carried a relA mutation.

Binding, Competitive↗
PubMed1978

Mutations in the tryptophanyl-transfer ribonucleic acid ligase of E. coli causing temperature-sensitivity for growth.

Strains of Escherichia coli K-12 with altered tryptophanyl-tRNA ligases, conferring temperature-sensitivity for growth, have been isolated as spontaneous one-step mutants. The mutated enzymes differ markedly in activity from the wildtype, even at the permissive temperature. When assayed at the non-permissive temperature, the mutant enzymes are completely inactive. In one of the mutant strains, growth can be completely inhibited by addition of L-phenylalanine or L-tyrosine to the medium.

Amino Acyl-tRNA Synthetases↗
PubMed1976

Assignment of a gene for tryptophanyl-transfer ribonucleic acid synthetase (E.C. 6.1.1.2) to human chromosome 14.

We describe a simple method for locating tryptophanyl-tRNA synthetase (E.C. 6.1.1.2) on cellulose acetate gels (Cellogel) following electrophoresis. Employing electrophoretic conditions which result in the separation of mouse and human tryptophanyl-tRNA synthetase, we have analyzed extracts of a number of independently derived mouse-human somatic cell hybrids and subclones derived from these hybrids for the presence of human tryptophanyl-tRNA synthetase. Electrophoretic patterns of hybrid extracts which contain human tryptophanyl-tRNA synthetase exhibit three bands. This is consistent with published evidence that the enzyme for mammalian cells is a homologous dimer. The electrophoretic patterns derived from some hybrids are unusual in that the human and hybrid bands of activity are more intense than the mouse band from the same hybrid. An analysis of hybrid cells and extracts indicates that human tryptophanyl-tRNA synthetase segregates with human chromosome 14 and with the only enzyme marker which has previously been assigned to this chromosome, nucleoside phosphorylase.

Amino Acyl-tRNA Synthetases↗
PubMed1976

Assignment of a human gene for tryptophanyl-tRNA synthetase to chromosome 14 using human-mouse somatic cell hybrids.

Human tryptophanyl-tRNA SYNTHETASE (Trp-RS, EC 6.1.1.2) can be separated from its mouse counterpart by Cellogel electrophoresis. Analysis of the presence or absence of human Trp-RS and other human enzyme markers in eleven independently dervied cell lines of human-mouse somatic cell hybrids revealed that the expression of Trp-RS is correlated with the expression of human nucleoside phosphorylase (NP, EC 2.4.2.1). The syntenic relationship between Trp-RS and NP permits the assignment of the structural gene for Trp-RS to human chromosome 14. Karyotype and isozyme analysis of these hybrid clones rules out other linkage assignments.

Amino Acyl-tRNA Synthetases↗
PubMed1977

Intrachromosomal gene mapping in man: the gene for tryptophyl-tRNA synthetase maps in region q21 leads to qter of chromosome 14.

A gene for tryptophanyl-tRNA synthetase (EC 6.1.1.2), the enzyme which attaches tryptophan to its tRNA, has previously been assigned to human chromosome 14 by analysis of man-mouse somatic cell hybrids. We report here a method for the electrophoretic separation of Chinese hamster and human tryptophanyl-tRNA synthetases and its application to a series of independently derived Chinese hamster-human hybrids in which part of the human chromosome 14 has been translocated to the human X chromosome. When this derivative der (X),t(X;14) (Xqter leads to Xp22::14q21 leads to 14qter) chromosome carrying the human gene for hypoxanthine-guanine phosphoribosyltransferase was selected for and against in cell hybrid lines by the appropriate selective conditions, the human tryptophanyl-tRNA synthetase activity was found to segregate concordantly. These results provide additional confirmation for the assignment of the tryptophanyl-tRNA synthetase gene to human chromosome 14 and define its intrachromosomal location in the region 14q21 leads to 14qter. Our findings indicate that the genes for tryptophanyl-tRNA synthetase and for ribosomal RNA are not closely linked on chromosome 14.

Amino Acyl-tRNA Synthetases↗