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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An isogenic pair of Escherichia coli mutants (relA+ tufB valSts and relA1 tufB valSts) has been cultured at several temperatures to establish various degrees of limitation for valyl-tRNA synthetase. The biosynthetic rate of 16 identifiable proteins, most of which are components of the transcription and translation apparatus, was measured by pulse-labelling with [35S]-methionine, followed by protein separation using two-dimensional gel electrophoresis (O'Farrell, 1975). No single pattern of response to amino acid starvation of biosynthetic rate was observed. EF-Ts, L12 and S6 were found to be under strong stringent and relaxed regulation; EF-G, EF-Tu-A and S1 are under strong stringent, but weak relaxed regulation; EF-Tu-B, alpha, VRS, IRS and ARS are under week stringent and weak relaxed regulation; beta is under weak stringent regulation and does not respond at all to relaxed conditions; the biosynthetic rate of a protein called stringent starvation protein is strongly stimulated, relative to other proteins, in the starved stringent strain.
Mol Gen Genet 1976 Dec 22
PMID:Biosynthetic regulation of individual proteins in relA+ and relA strains of Escherichia coli during amino acid starvation. 79 46

The N-terminal sequences of the separated polypeptide chains of biliproteins isolated from several Cyanophyta, Rhodophyta, and Cryptophyta have been determined. The portions of the sequences determined for the alpha (fast) chain of C-phycocyanin from both procaryotic and eucaryotic cells are extremely conservative. Methionine is the N-terminal amino acid in most of the species studied. The N-terminus and subsequent sequence of phycoerythrin alpha chains are almost identical with those of the C-phycocyanin alpha chain. The beta (slow) chain of C-phycocyanin is also rather conservative in amino acid substitution but has more variation than the alpha chain. The variations are consistent with single base changes in codons and conserve the size and functional characteristics of the amino acid. The sequence homologies are consistent with the phylogenetic relationship between Cyanophyta and the chloroplast of Rhodophyta. There are no other reported sequences of polypeptide chains of the same or related proteins from such different strains of microorganisms that show such close sequence homology.
J Mol Evol 1975 Jul 11
PMID:Letter: Sequences of the N-terminus portions of biliproteins. 80 32

The in vitro B. subtilis protein synthesizing system is very restricted in its ability to translate E. coli phage messenger RNA's, specifically phage T4 RNA, even though it actively translates its proper mRNA species. In contrast, the E. coli system translates with similar efficiency mRNA from either source. The initiation factors from the two systems are functionally interchangeable. The 30S B. subtilis ribosomal subunit is responsible for the limited template specificity of the B. subtilis ribosomes. Although the efficiency of the T4RNA directed F Met-tRNA binding by B. subtilis ribosomes is less than that of SPOI RNA-directed binding, the most restrictive step in the translation of T4RNA by B. subtilis ribosomes appears to be at the level of the formation of the first peptide bond, as measured by F Metpuromycin formation.
Mol Gen Genet 1976 Dec 31
PMID:Selective messenger translation by Bacillus subtilis ribosomes. 81 1

Newly synthesized non-histone proteins (NHP) labelled with [35S] methionine were isolated from uterine epithelium and stroma after different hormone treatments and examined by isoelectric focusing in polyacrylamide gels. Progesterone increased the proportion of basic NHP in the epithelium. This effect was detectable within 4 h and was maintained unchanged after oestrogen stimulation, which increased the synthesis of all classes of NHP. The proportion of basic NHP was higher in the untreated stroma than in the epithelium. Progesterone pretreatment did not increase the proportion of basic NHP in the stroma but prevented the increase in the more acidic NHP which followed treatment with oestrogen alone. The tendency to synthesize a higher proportion of basic NHP did not in any way correlate with the tissue's proliferative status.
Mol Cell Endocrinol 1977 Jan
PMID:The effects of sex-steroids on the synthesis of uterine non-histone proteins. 83 65

Protoplasts of methionine- and lysine-requiring h- mutants isolated from the L972 h- strain of Schizosaccharomyces pombe were fused. The protoplasts were obtained from the cells with enzymes produced by Trichoderma viride. When a mixture of the protoplasts was treated with 30% PEG 4000 solution containing 10 mM CaCl2, cell fusion and complementation was attained with a frequency of 0.17%. Both fusion partners were recovered among the spores after crossing of the fusion products with the strain M210 ade6 h+. Cytological and haploidization examinations showed that the fusion cells are not heterokaryons, and that the increased amount of genetic material is situated in one nucleus.
Mol Gen Genet 1977 Feb 28
PMID:Protoplast fusion of Schizosaccharomyces pombe Auxotrophic mutants of identical mating-type. 86 81

Rat liver ribosome treatment with ethanol and 1 M NH4Cl releases some 31-33 ribosomal proteins. This split protein fraction binds Phe-tRNA, Ac-Phe-tRNA, Met-tRNAM and f-Met-tRNAF in the absence of K+ and Mg++ ions. When the split protein fraction is passed through Sephadex G-100 only six proteins are retained in the column: S10, S14, S15, S19, L35, and L36. The aminoacyl-tRNA binding activity of this protein fraction retained in the Sephadex G-100 column is similar to that of the total split protein fraction, suggesting that the above six proteins, or only some of them, are involved in the binding reaction.
Mol Biol Rep 1976 Jul
PMID:Binding of aminoacyl-tRNA to rat liver ribosomal proteins. 95 16

We find that specific oxidation for the Met-192 residue in delta-chymotrypsin to methionine sulfoxide results in a twofold increase in Km(app) and unchanged kcat in the hydrolysis of N-acetyl mono(amino acid) amide substrates. However, the catalyzed hydrolyses of N-acetyl dipeptide amide substrates by (methionine sulfoxide)-192-delta-chymotrypsin (MS-delta-Cht) shows a four- to fivefold decrease in kcat and unchanged Km(app) with respect to delta-chymotrypsin. Hydrolysis of alpha-casein by MS-delta-Cht shows a similar 4.2-fold decrease in kcat. These results imply that the Met-192 acts differently with substrates that bind only in the primary, S1, binding site (i.e., AcPheNH2) from those that bind to more extended regions of the enzyme active site. In the binding of c+AcPheNH2 and AcTrpNH2, the results support a mechanism in which the Met-192 acts to slow the rate of sustrate dissociation from the Michaelis complex to free substrate and enzyme. This is in agreement with the x-ray crystallographic structure of dioxane inhibited alpha-chymotrypsin (Steitz, T., et al. (1969), J. Mol. Biol. 46, 337). However, this mechanism is not apparent when peptide and protein substrates bind. The decrease in kcat on Met-192 modification of approximately fivefold in the hydrolysis of polypeptide substrates show a small, but significant, catalytic contribution of the Met-192 toward the lowering of the energy of activation polypeptide substrate hydrolysis by chymotrypsin. This may support the crystallographic model of Fersht et al. (Fersht, A., et al. (1973), Biochemistry 12, 2035) in which it is proposed that the Met-192 participates in the distortion of bound polypeptide substrates toward the reaction transition-state configuration and, thus, plays a role in catalysis. However, if this mechanism occurs, the effect is small, only contributing about 1 kcal/mol to the lowering of the reaction activation energy.
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PMID:The role of methionine-192 of the chymotrypsin active site in the binding and catalysis of mono(amino acid) and peptide substrates. 96 30

Proteins present in messenger ribonucleoprotein particles were labeled with [35S]-methionine in Ehrlich ascites tumor cells in which synthesis of new ribosomes was inhibited. Poly(A)-protein complexes were isolated from free and membrane-bound polyribosomes by sucrose gradient centrifugation and affinity chromatography on oligo(dT)-cellulose. Both classes of Poly(A)-protein particles contain a poly(A) chain of about 70 adenyl residues and a protein with a molecular weight of 76000 attached to it.
Mol Biol Rep 1976 Sep
PMID:Characterization of poly(A)-protein complexes isolated from free and membrane-bound polyribosomes of Ehrlich ascites tumor cells. 103 5

1. Methionine adenosyltransferase (ATP:L-methionine-S-adenosyl transferase, EC 2.5.1.6), cystathionine beta-synthase F1L-serine hydro-lyase (adding homocysteine), EC 4.2.1.22] and cystathionine gamma-lyase [L-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1] activities were found only in the cytosol fraction of rat liver cells. None was found in the mitochondrial or endoplasmic reticulum fractions as judged by the distribution of marker enzymes on a density gradient after centrifugation of the cytoplasmic fraction of a liver homogenate, or in a preparation of liver cell nuclei. 2. Polymorphs, lymphocytes (with admixed monocytes) and mixed bone marrow white cells contained no methionine adenosyl transferase, cystathionine beta-synthase or cystathionine gamma-lyase activities. 3. The possible bearing of these results on the problem of abnormal cystine storage in cystinosis is briefly discussed.
Clin Sci Mol Med Suppl 1975 Jun
PMID:Methionine adenosyltransferase, cystathionine beta-synthase and cystathionine gamma-lyase activity of rat liver subcellular particles, human blood cells and mixed white cells from rat bone marrow. 105 81

In order to analyse how many structural genes are implicated in the specific steps of the biosynthesis of methionine in Sacch. cerevisiae, a hundred mutants were studied by complementation. 21 groups were defined named MET1 to MET25. Neither recombination between independent mutants of the same complementation group nor linkage between different groups was found. Preliminary to biochemical studies, mutants of each complementation group were tested for their capacity to utilize various precursors of methionine.
Mol Gen Genet 1975 Aug 05
PMID:Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants. 110 Oct 32


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