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

Fractionation of acid-soluble proteins from yeast Saccharomyces cerevisiae chromatin by gel electrophoresis suggested the existence of four histonestone fractions--H2a, H2b, H3, H4 and histone H1-like protein. The latter was isolated according to the second method of Johns and extracted with 5% HClO4. Amino acid analysis of the histone H1-like protein showed a moderately high content of basic amino acids, but a much lower ratio of lysine: arginine (approximately 3) than that of the hisone H1 from higher eukaryotes. In addition to histone H1-like protein a protein X was also extracted with 5% HC1O4. The sequence of the electrophoretic mobilities of histone fractions from yeast coincides with those of histone fractions from plants--H4 greater than H3 greater than H2a greater than H2b greater than H1.
Mol Biol (Mosk)
PMID:[Electrophoretic study of the acid soluble proteins of Saccharomyces cerevisiae yeast chromatin]. 35 66

The effect of 2,4-pentandione on the activity of phenylalanyl-tRNA synthetase (Phe-RSase) from E. coli MRE-600 was investigated. It was shown that modification of Phe-RSase with 2,4-pentandione leads to decrease of the aminoacylation rate without an influence on the ATP--[32P]pyrophosphate exchange reaction rate. tRNAPhe protects the enzyme against inactivation. Neither L-Phe and ATP nor the analog fo aminoacyladenylate protects the enzyme against inactivation. There are no changes in Km for amino acid and ATP in the aminoacylation reaction after modification while Km for tRNAPhe decreases three times. The dissociation constant of Phe-RSase: [14C]Phe-tRNA complex increases 4--8 times after modification. It is assumed that there are some lysine residues in Phe-RSase essential for the Phe-RSase-tRNA interaction.
Mol Biol (Mosk)
PMID:[Role of the lysine residues in the phenylalanyl-tRNA synthetase substrates interaction]. 36 1

The influence of modification of Phe-RSase from E. coli MRE-600 by lysine- and arginine-specific reagent 2,4-pentandione on the Phe-RSase.tRNAPhe interactions was investigated. It was shown that modification of Phe-RSase with 2,4-pentandion leads to a decrease of the aminoacylation rate without any influence on the value of Km for tRNAPhe in this reaction and only a slight increase of the value of Kdiss for Phe-RSase.tRNAPhe complex. The log Km (Km-1)--ionic strength dependence for native enzyme and log Kdiss (K-1diss) for native enzyme and two forms modified on arginine and lysine residues were investigated. Results were interpreted quantitatively by Debye--Huckel approximation for two spherical macroions and by Daune approximation assuming that the region of tRNA implicated in ionic interactions is locally a cylindrical polyelectrolyte. It was shown that there are 2-4 electrostatic contacts in Phe-RSase.tRNAPhe interactions in limits of both approximations; modification of arginine residues in Phe-RSase doesn't change the number of electrostatic contacts, modification of lysine residues leads to an increase in the number of contacts. It was assumed that there are lysine residues in Phe-RSase essential for the tRNAPhe recognition. The possibility of participation of negative amino acid residues in electrostatic interactions with tRNAPhe is not excluded.
Mol Biol (Mosk)
PMID:[Influence of the modification of Phe-tRNA synthetase from Escherichia coli by lysine- and arginine-specific reagent on the ionic interactions of the enzyme with tRNA Phe]. 38 96

The interaction of pyridoxal, pyridoxal-5'-mono-, di- and triphosphate with certain enzymes of polynucleotide synthesis (DNA-dependent RNA polymerase, DNA-dependent DNA polymerase I and polynucleotide phosphorylase from Escherichia coli and terminal deoxyribonucleotide transferase from calf thymus) was studied. All compounds tested was found to be reversible and competitive inhibitors of these enzymes. The reduction of the enzyme-inhibitor complex with NaBH4 gives rise to the complete irreversible inhibition of the enzymes under study. The comparison of the inhibition constants for pyridoxal and its phosphorylated derivatives with those for mono-, di- and triphosphates of nucleosides was carried out for the enzymes. The results obtained suggest that the modified epsilon-amino-group of lysine residue should be localized at the catalytic site in the vicinity of the pyrophosphate binding area of an enzyme.
Mol Biol (Mosk)
PMID:[Interaction of oligophosphates of pyridoxal with certain enzymes of polynucleotide synthesis]. 38 98

We have analyzed some chemical properties of the sigma subunit of RNA polymerase from the sigma mutants: rpoD1 (Gross et al., 1978), rpoD2 (formerly known as alt-1) (Silverstone et al., 1972; Travers et al., 1978), and rpoD800 (Gross et al., 1979). Each of the three mutants is located at about 66 min on the E. coli genetic map and exhibits an alteration in the enzymatic properties of its sigma subunit. The tryptic peptides and isoelectric focusing behavior were analyzed for mutant and wild type sigma. A single, but different altered lysine tryptic peptide was observed for each mutant. No altered arginine tryptic peptides were observed. The rpoD800 mutant sigma showed an altered isoelectric point. These studies provide chemical evidence that the sigma polypeptide in all three mutants is altered and strongly support the conclusion that the mutations are in the structural gene for sigma.
Mol Gen Genet 1979 Oct 01
PMID:Altered chemical properties in three mutants of E. coli RNA polymerase sigma subunit. 39 26

Nuclear 30S RNP particles were studied by means of fluorescence techniques. It's shown that fluorescamin interacts with NH2-groups of protein molecule. As a result, covalent fluorescent label is formed. Quantum yield (rho), fluorescence spectra, lifetime of excited state (tau) and polarization of fluorescamin complexes with 30S particles were studied. Excitation spectra have their maximum at 395 nm, and fluorescence spectrum at 480 nm. These figures correspond to spectra of fluorescamin complexes with NH2-groups of lysine. Mean quantum yield (rho = 0.27) and lifetime of excited state of fluorescence (tau = 7.8 nsec) were measured. It's shown that fluorescamin forms two types of fluorescent complexes in 30S particles. These complexes differ only by their rho(rho1 = 0.11, rho2 = 0.30) and rho(rho1 = 3.6 nsec, rho2 = 10.0 nsec) by 2.7 times. Migration radius between fluorescamin bound to protein and ethydium bromide adsorbed on double-stranded regions of pre-mRNA in RNP-particles was measured. It's equal to 32 A. Adsorbtion isotherms of ethydium bromide were measured by fluorescence in 0.1 and 0.4 M NaCl. Data obtained showed that 6% of pre-mRNA in 30S particles bound the dye as a strong complex, i. e. this part of pre-mRNA is double-stranded. RNase treatment of RNP had no effect on this value. But the increase of NaCl concentration up to 0.4 M caused the dissociation of protein subunits to some extent followed by appearance of up to 40% free NH2-groups interacting with fluorescamin. Measuring of energy migration from fluorescamin to ethydium bromide showed that double-stranded pre-mRNA regions strictly bound to protein sticked out from RNP particle at a distance of about 27 A. The increase of NaCl concentration up to 0.4 M leads to disruption of this strict bond of double-stranded regions with protein. As a result, these regions of pre-mRNA become labile and move away from the RNP particle at more than 30 A. According to theoretical calculations, there is about 1--2 pre-mRNA hairpins (18--9 base pairs respectively) per one 30S particle.
Mol Biol (Mosk)
PMID:[Nuclear ribonucleoproteins containing pro-mRNA. XIV. Structural study using ethidium and fluorescamine]. 44 Mar 9

Protein biosynthesis in neurointermediate lobes of mouse pituitaries was investigated using pulse and pulse-chase techniques with [3H]lysine. Electrophoretic analysis of lobe homogenates on acid-urea gels resolved 11 labeled products. One was a large protein which was rapidly synthesized during pulse-incubations and disappeared during chase incubations. Three of the products increased during chase incubations, suggesting a precursor-product mode of biosynthesis for these chasde peptides. One of these three products co-migrated with synthetic alpha-MSH and also corresponds to the major peak of mouse neurointermediate lobe MSH bioactivity and immunoactivity on electrophoretograms. Another case of these peptides has electrophoretic properties similar to those of ACTH.
Mol Cell Endocrinol 1979 Feb
PMID:Biosynthesis of MSH and related peptides in the pars intermedia of the mouse: a pulse-chase analysis. 44 80

A series of five alternating poly(leucyl-lysyl) samples with varying amounts of L-and D-residues randomly distributed along the chain, but evenly shared out amongst leucyl and lysyl residues were synthesized by condensation of a mixture of the four diastereoisomeric dipeptide p-nitro-phenylesters. Their behavior in aqueous solution at various ionic strengths was studied by infrared spectroscopy which allowed measurement of the total amount of beta-structures, and by circular dichroism which gives the excess of L-residues over D-residues in the same structures. Comparison with the properties of the all L-poly(Lys-Leu-Lys-Leu) shows that incorporation of a few D-residues in a L-chain seems to reduce the width of the beta-sheets obtained in presence of salt. Higher proportions of D-isomers prevent the coil leads to beta transition from occurring when the ionic strength is increased except for segments containing at least 6 to 7 adjacent residues of the same configuration.
J Mol Evol 1979 Jun 08
PMID:Beta-structures of polypeptides with L-and D-residues. Part I. Synthesis and conformational studies. 45 71

Cell-free protein synthesizing systems were prepared from the livers of chick embryos at selected ages and the characteristics of individual fractions were compared. While polysomes showed decreasing size with older embryos, isolated polysomes did not differ significantly in amino acid incorporating activity when assayed with standard cell sap. When assayed with standard polysomes, cell sap activity decreased with increasing developmental age whether incorporation was measured using (3H)lysine, (3H)leucine, or [3H]aminoacyl-tRNA. Free amino acid concentrations in the cell sap showed reproducidble independent variation during development which was taken into consideration in calculating net amino acid incorporation. A larger increase in ribonuclease activity was observed during development; however, nuclease inhibitor activity was absent before day 15 but increased thereafter. Aminoacyl-tRNA sythetase activity did not vary significantly. It is proposed that the observed changes in the rate of cell-free protein synthesis result not only from increasing ribonuclease activity with increasing developmental age but also from changes in the activity of other soluble factors.
Mol Cell Biochem 1979 Apr 02
PMID:Polymorphism in fowl serum albumin. VI. Changes in in vitro protein synthesizing activity in developing embryonic fowl liver. 46 Jan 76

Nucleotide derivatives (epsilon-amino groups of lysine residues) of lysine residues) of poly(oligo)-L-lysine were synthesized. The structure of the resulting compounds in solution were studied by circular dichroism techniques. Week stacking interactions of the nucleotide bases on the polypeptide template were found to be characteristic of these compounds. It has been shown that the nucleotide derivatives of poly(oligo)-L-lysine are not involved in complementary interactions with the polynucleotides.
Mol Biol (Mosk)
PMID:[Synthesis and properties of nucleotide derivatives of poly(oligo)-L-lysine]. 46 Feb 5


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