Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A chromatin with the protein/DNA ratio of 3.0 was obtained from rat liver cells nuclei. The chromatin was dissolved in 2 M NaCl, pH 7, and reprecipitated by decreasing the ionic strength to 0.4 and increasing pH to 9.0. A fraction of non-histone proteins (NH-1) remained in a supernatant solution, the NH-1/DNA ratio being equal to 1.3 and the ratio of acidic to basic aminoacid residues equal to 1.31. After chromatography on Bio-Rex 70 cation-exchang resin, a fraction (NH-2) with the NH-2/DNA ratio of 1.0 +/- 0.15 and the ratio of acidic to basic aminoacid residues of 1.57 was obtained. According to the data of polyacrylamide gel electrophoresis, the NH-2 fraction contained 2.7% of histone f2 + f3 as an admixture whereas histone f1 was not revealed.
Mol Biol (Mosk)
PMID:[Isolation of rat liver chromatin non-histone protein]. 0 62

Comparative studies have been carried out for the chemical composition and physico-chemical characteristics of chromatin isolated from spleens of non-immunized and immunized mice. It is found that the chromatin from spleens of immunized mice contains significantly more non-histone proteins and RNA, while the quantity of histone proteins is unaltered. The melting temperatures of chromatin from spleens of non-immunized and immunized mice in 2.5-10(-4) M EDTA (pH 8.0) are 76.8+/-1.50 degrees and 74.4+/-1.10 degrees, respectively. DNA isolated from chromatin melts at 40 degrees. The melting of chromatin was followed in 5 mM sodium-cacodylate buffer (pH 7.0)+1.5-10(-4) M EDTA containing increasing concentrations of urea. The results show that during immunogenesis the changes of the chemical composition of the chromatin are accompanied by certain destabilisation of DNP complex.
Mol Biol (Mosk)
PMID:[Changes in the chemical composition and physico-chemical characteristics of chromatin from spleens of mice during immunogenesis]. 0 29

The deficiency of the 38B-40 region containing histone genes in one of the 2nd chromosomes of D. melanogaster triploid intersexes increases the template activity of X-chromosomes both in vivo and in vitro without noticeably affecting autosome activity. This deficiency in the heterozygous state inhibits the variegated position effect of the white gene in the T(1;3)Wvco translocation in diploid females and males, but not affect their rate of development. The variegation suppressor Su(var)hg-1 not only suppress the gene position effect in diploid flies, but also increases the template activity of X-chromosomes in triploid intersexes. The results are discussed with respect to the dependence of gene activity on the structure of chromosomes (density of DNP packing).
Mol Gen Genet 1978 Jul 04
PMID:Influence of deficiency of the histone gene-containing 38B-40 region on X-chromosome template activity and the white gene position effect variegation in Drosophila melanogaster. 9 1

Under experimental conditions of genetic transformation, protamine and total histone were bactericidal for Bacillus subtilis cells. The abilities to cause lethality were very similar for both, either protamine or histone, with no antagonistic effects amongst these natural polycations. With both basic proteins acting simultaneously the enhancement was higher than a summation of the separate lethal effects. Sublethal concentration of protamine added at the beginning of transformation time, produced a strong inhibition of transforming efficiency. The same concentration added later than 10 min from the start of transformation had no inhibitory effect. These facts together with the absence of inhibition by simple pretreatment of DNA alone as well as the cell protection by protamine against lytic activity of lysozyme, suggest a protamine-cell surface interaction which impedes DNA uptake events.
Mol Gen Genet 1979 Mar 05
PMID:Lethal effect of protamine and histone on competent Bacillus subtilis cells. Inhibition of genetic transformation by protamine in sublethal concentration. 11 Oct 2

The influence of a specific histone kinase, phosphorylating lysine-rich histone F1, F2a2, F2b, on the physico-chemical properties of the chromatin in the whole undestroyed fixed cell, has been investigated. It was found that the exogenous histone kinase penetrates into the nuclei of the undestroyed fixed cells and into the isolated unfixed nuclei and changes the physico-chemical properties of the chromatin there, bringing about an increase in binding of a basic dye acridine orange and a decrease in its stability to heat.
Mol Biol Rep 1975 Oct
PMID:Influence of a specific histone kinase on the physico-chemical properties of chromatin in situ. 17 82

The phosphorylation of lysine-rich histones F1, F2a2 and F2b of calf thymus has been investigated using homogeneous histone kinase from pig brain. 32P-labelled phosphopeptides from tryptic digests of corresponding histones were obtained. According to N-terminal analysis and the quantitative determination of amino acid composition of the obtained radioactive peptides the sites of phosphorylation were identified in the primary structure of lysine-rich histones, namely, Ser-38 for the polypeptide chain of histone F1, Ser-19 or 18 for histone F2a2 and Ser-14 and 36 for histone F2b. Thus, the high specificity of brain histone kinase in vitro was demonstrated.
Mol Biol (Mosk)
PMID:[Phosphorylation of lysine-rich histones by swine brain histokinase]. 18 71

The protein kinase of normal human adrenal cytosol has been resolved by DEAE-cellulose chromatography into two major components, the protein kinases I and II, which are both adenosine 3',5'-monophosphate (cAMP) dependent. Both enzymes have similar substrate specificities, cAMP-dependency, and sensitivity to the stimulation by this nucleotide, but differ in their states of activation after preincubation with histone. The DEAE--cellulose charomatography of dissociated cytosol protein kinase reveals only one peak of kinase activity and two peaks of cAMP binding activity (A and B). Both binding proteins are able to inhibit the kinase activity of the catalytic subunit. Recombination experiments suggest that the regulatory subunit A originated from protein kinase I and subunit B from protein kinase II. The phosphorylation of histone by adrenal protein kinases is inhibited by a heat-stable protein inhibitor isolated from human fetal brain and human adult adrenal.
Mol Cell Endocrinol 1977 Jan
PMID:Adenosine 3',5'-monophosphate-dependent protein kinase from normal human adrenal. 18 3

A heat-and acid-stable protein inhibitor of phosphorylase phosphatase is present in a highly purified preparation of protein inhibitor of cyclic AMP-dependent protein kinase from rabbit skeletal muscle. Although these two inhibitors have strikingly similar properties to each other, such as sensitivity to trypsin and behavior on gel permeation chromatography, they can be separated by polyacrylamide disc gel electrophoresis. This indicates that the phosphatase-inhibitory and kinase-inhibitory activities reside with different protein species. The inhibition of both the enzymes is not altered by incubating the inhibitor preparation with a general phosphoprotein phosphatase, with phosvitin kinase, or with cyclic AMP-dependent protein kinase. Inhibition of phosphorylase phosphatase is of a non-competitive type supporting the idea that the phosphatase inhibitor is not an alternative substrate for the enzyme. Inhibition of phosphatase activity is selective in that it does no occur when phosphorylated histone or phosphorylated protamine are used as substrates.
Mol Cell Biochem 1977 Apr 12
PMID:Protein inhibitors of phosphorylase phosphatase and cyclic AMP-dependent protein kinase from rabbit skeleta muscle. 19 98

Thyroxine control of cAMP-independent histone and casein phosphokinase activities was studied in thyroidectomized rats treated with thyroxine. All activities were evaluated in the presence of a thermostable inhibitor of cAMP-dependent enzymes. Cytosol enzymes can be resolved by sucrose gradient ultracentrifugation into three peaks of histone kinase activity (3.2S, 5S and 7.2S) and two peaks of casein kinases (3.6S and 7.1S). Neither thyroidectomy nor subsequent treatment of operated animals with thyroxine modifies the total histone kinase activity estimated, either in total cytosol or after its fractionation by the sucrose gradient ultracentrifugation. The activity ratios of different peaks were, however, changed. Casein kinase activity was significantly decreased after thyroidectomy (about 50%). Subsequent treatment with thyroxine restored this activity to its initial value. Sucrose gradient ultracentrifugation analysis showed that thyroxine action on the casein kinase activity is very specific. Only molecules that sediment in the 9S region were significantly stimulated by the hormone. Cortisol action on the casein kinase activity was studied in adrenalectomized animals treated with hormone for 24 h. Cortisol decreases the total casein kinase activity by about 30%. Sucrose gradient ultracentrifugation analysis showed that the population of molecules sedimenting at about 9S was the most sensitive to cortisol. The above data show that both thyroxine and cortisol control, in a selective way, the activities of cAMP-independent protein kinases. The same kinase molecules can be under double control by two different hormones that have opposite effects.
Mol Cell Endocrinol 1978 Dec
PMID:Hormonal regulation of cAMP-independent protein phosphokinase activities: thyroxine and cortisol control of enzymes from rat liver cytosol. 21 94

The effect of mengovirus infection on the extent of phosphorylation of histone H1 was studied in Ehrlich ascites tumor cells. After prelabeling of the nuclear protein with [32P] orthophosphate, the excorporation of radioactivity was followed as a function of time postinfection. Employing high-resolution polyacrylamide gradient slab gel electrophoresis and autoradiography, it was found that, compared to a relatively slow turnover of phosphate groups in histone H1 in mock-infected cells, in mengovirus-infected cells the excorporation of radiolabel from histone H1 was significantly enhanced. In the latter case, the decrease of histone-bound radioactivity was paralleled by a reduction of the band multiplicity in the histone H1 region of the electrophoresis profile. It was also shown that the microheterogeneity in the histone H1 complements isolated at various times postinfection was reduced to the same basal 3-band level by incubation of the nuclear protein fractions in the presence of alkaline phosphatase. After this treatment, the band multiplicity equaled that found in histone H1 from stationary cells.
Mol Biol Rep 1978 Oct 16
PMID:Dephosphorylation of histone H1 after mengovirus infection of Ehrlich ascites tumor cells. 21 3


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