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

The problem to be reviewed in this study concerns the mechanism of regulation of gene activity relied on the structural changes of the chromatin. The role of histones in the regulation of transcription is discussed on the basis of the results obtained by the authors and literature data. In particular, the results are presented of the investigations of decrease of the histone amount in the cell nucleus using the deficiency of histone structural genes. This leads both to the increase of the X-chromosome template activity and the inhibition of variegated position effect. The latter is also inhibited by feeding of larvae with T2-DNA. It is supposed that the chromatin structure is a mechanism of epigenetic changes and the gene inactivation due to the position effect inherited in cell lineages in an example of such epigenetic changes.
Mol Biol (Mosk)
PMID:[Chromosome structure, histones and gene activity in Drosophila]. 78 38

Chromosomal non-histone proteins are obtained from nuclei of two types of pigeon erythroid cells: erythroblasts (cells active in RNA synthesis) and erythrocytes (cells with repressed RNA synthesis). They are well soluble in solutions of low ionic strength. Electrophoretic separation of the obtained non-histone proteins in polyacrylamide gels with urea and SDS shows the presence of qualitative differences in the pattern of non-histone proteins of chromatine from erythroblasts and erythrocytes. By electrophoresis in urea some protein bands of non-histone proteins of chromatine from erythroblasts were found which disappear with the aging of cells. At the same time two protein fractions were observed in chromatine from erythrocytes which were absent in that of erythroblasts. Disappearance of some high molecular weight protein fractions from erythrocyte chromatine as compared to erythroblasts was observed by separation of the non-histone proteins in the presence of SDS. These fractions of the non-histone proteins disappearing during aging of cells are well extractable from erythroblast chromatine by 0.35 M NaCl solution. In the in vitro system with E. coli RNA polymerase addition of non-histone proteins of chromatine from erythroblasts to chromatine from erythrocytes increases RNA synthesis 2--3 times. At the same time addition of non-histone proteins from erythrocytes is either without any influence on this process or somewhat inhibiting.
Mol Biol (Mosk)
PMID:[Comparative investigation of the non-histone proteins of chromatin from pigeon erythroblasts and erythrocytes]. 80 71

The occurence of the basic chromosomal proteins in lower eukaryotes provides a useful approach to the study of histone evolution and function in higher eukaryotes. The histones of higher plants and animals are very similar and some are nearly identical, suggesting a high degree of evolutionary conservation within this group of proteins. However, a literature survey reveals that in the lower eukaryotes the histone situation is quite variable. The ciliates, and the true and cellular slime molds possess basic chromosomal proteins that are very similar to the histones of higher plants and animals. Various other lower eukaryotes possess basic chromosomal proteins that resemble at least some of the major histone fractions, and some microorganisms possess basic chromosomal proteins that bear little or no relationship to higher plant and animal histones. Since histones play a major role in the control of gene expression and the maintenance of chromosome structure in higher organisms, the evolution of these proteins represents a major change in the packaging of DNA and the mode of regulating gene expression in eukaryotes.
J Mol Evol 1976 Jun 23
PMID:Basic chromosomal proteins in lower eukaryotes: relevance to the evolution and function of histones. 82 Aug 66

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

Non-histone proteins from chromatin of sea urchin embryos were found to possess the ability to agglutinate erythrocytes.
Mol Biol Rep 1977 Jun
PMID:Lectin activity of chromatin non-histone proteins. 88 96

Homologous whole histone from calf thymus was adsorbed on Sepharose 4B columns with covalently coupled histone fractions H2a, H2b, H3 or H4 in 0.01 M phosphate buffer, pH 6.7 - 1 M NaCl. The adsorbed histones were eluted from the columns with 5 M urea in the same buffer. Electrophoretic analysis has shown that the different columns exhibit selective affinity to the histone fractions: the H2b column to histone H2b and H2a (with only weak affinity to histones H3 and H4), the H2a column to histones H2b and H3 (moderate affinity to histone H2b), and the H4 column to histone H3, H4 and H2b (weak affinity to histone H2a). Histone H1 displayed no fixation by either of the columns tested.
Mol Biol Rep 1976 Sep
PMID:A study of histone-histone interactions by affinity chromatography. 100 3

The subfraction composition of lysine-rich histone has been studied with the aid of polyacrylamide gel electrophoresis. The subfraction compositions of the histone F1 of several tissues from the chicken, pigeon, and titmouse have been compared. The histone F1 from the tissues investigated consists of four or five subfractions of similar number and electrophoretic mobility (1, 1a, 2, 3, and 4). In the different avian species each subfraction varied its mobility independently of the others. The chicken tissues investigated can be divided into two classes, depending on the relative concentration of subfractions 2 and 3 (A and B): Class A (subfraction 2 is smaller than 3) includes the brain, liver, skeletal muscle, heart, muscular layer of the stomach, and pancreas, and class B (subfraction 2 is larger than 3) includes the intestinal mucosa, thymus, and testes, as well as the liver, heart, and pancreas from a 21-day embryo. Such a division of the tissues corresponds to the varying rate of their cellular renewal. In a parallel examination of the relative concentrations of the individual subfractions in the same tissues from the three avian species it has been found that the relative concentration of subfractions 3 and 2 is increased in the skeletal muscles, heart, brain, and liver, that subfraction 2 is increased in the intestinal mucosa, that subfractions 4 and 3 are increased in the pancreas, and that subfractions 1, 1a, and 4 are increased in the erythrocytes. The results obtained may be interpreted as a consequence of some relationship between the subfraction composition of histone F1 and the type of tissue of the source.
Mol Biol (Mosk)
PMID:Study of the relationship between the subfraction composition of histone F1 and the type of tissue in birds. 102 52

A peptidic effector from calf thymus causes a strong stabilization of DNA double-stranded molecule in vitro. The active factor was isolated from aqueous ultrafiltered thymus extracts and purified by means of chromatography on DEAE-cellulose and then on Dowex 50 WX2. The purified thymic factor was characterized as a peptide of low molecular weight (less than 5000). The biological activity of the thymic factor cannot be attributed to a histone fragment. Melting data of the control DNA and of the DNA-active factor complex in various conditions of ionic strength and dielectric constant of the solution medium are recorded.
Mol Biol Rep 1976 Sep
PMID:Stabilization of double-stranded DNA molecule by non-histone peptidic effector from calf thymus. 103 3

Characteristic viscosity, sedimentation constant and optical anisotropy were studied of the complexes formed between DNA and histone fractions F3 and F3+F2a2. The parameters mentioned continuously change with the increase of protein content within the complex. Analysis of experimental data shows that binding of a histone bads to a decrease of size and thermodynamic rigidity of the DNA molecule. On the basis of results obtained a model of F3 histone binding with DNA is suggested, amino acid sequence of this protein being taken into account. Comparison of behaviour of nucleohistones DNA+F3 and DNA+F1 studied previously testifies different way of binding of these histones to DNA.
Mol Biol (Mosk)
PMID:[Investigation of DNA complexes with histones F3 and F3+F2a2]. 105 37

The kinetics of nitration of tyrosine residues in histones F1 and F2a1 by tetranitromethane has been investigated. At low ionic strength and 30-fold molar excess of nitrating agent the nitration reaction results in fast modification of all tyrosine residues in both histones. At the same time the rates of modification of different tyrosine residues in histone F2a1 are not identical and markedly exceed the rate of N-Ac-OEt-Tyr nitration in a model system. The increase of reaction mixture ionic strength causes an increase of modification rates. The differential UV-absorption spectra of histone F1 obtained by temperature perturbation show an abnormal positive characteristic maximum at 286.8 nm. Analysis of the dependence of nitration rates of tyrosine residues in histones in saline solutions upon the ionic strength and of difference UV-absorption spectra of histones leads to a conclusion that there are specific interactions of definite parts of histone polypeptide chains. These interactions may arise from aggregation of histone molecules.
Mol Biol (Mosk)
PMID:[Tyrosine residues in histones. Kinetics of histones F1 and F2A1 nitration by tetranitromethane]. 105 46


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