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

Two minor basic protein components (M1 and M2) were found in the histone extract from chromatin of pea seedlings. In the histone extract of pea cotyledons only one minor component (M1) was detected. These minor components show a high affinity for chromatin, have a molecular weight of 20.200 and 17.800 respectively and a basic amino acid composition. They are not contaminants of cytoplasmatic origin. Two similar minor components were found in the chromatin of Pisum arvense and Lens culinaris-seedlings, one component was present in the chromatin from cotyledons of these species.
Mol Cell Biochem 1979 Sep 28
PMID:The presence of minor histone components in the chromatin of Pisum sativum L. seedlings. 51 65

When histone is oxidized by peroxidase, its basicity (hence its complexing with DNA) is reduced: this reduction causes further alterations in the effect of histone upon the heat denaturation, acid precipitation, and breakdown by DNase of DNA, alterations which indicate that the regulation by histone of DNA expression may become abnormal. If oxidized species of histone should accumulate in the tissues in old age, the alteration mentioned might be a contributory factor of senescence.
Mol Biol Rep 1979 Dec 31
PMID:Histone: oxidation by peroxidase alters its interaction with DNA. 53 Feb 75

Electrophoretic mobility, amino acid composition and salt dissociation of histones isolated from sperm of sea urchin Strongylocentrotus intermedius and calf thymus cells were studied. The special arginine-rich histone fraction (I) has been observed in sea urchin sperm chromatin, this fraction being absent in calf thymus chromatin. Dissociation of lysine-containing histone fractions from sea urchin chromatin occured in the range of 0.7 to 1.0 M NaCl concentrations. H1 of calf thymus chromatin was totally extracted with 0.6 M NaCl. In the course of a further increase of salt concentrations (up to 1.5 M NaCl) a practically total extraction of histones from sperm chromatin was observed, while about 20% of proteins remained bound to DNA in thymus chromatin after extraction with 2.0 M NaCl. The template activity of non-extracted DNP preparations from urchin sperm was equal to 2-3% of that of totally deproteinized DNA. The template activity of DNP gradually increased at protein extraction from DNP preparations. The hybridization capacity of RNA transcribed on partially dehistonized DNP templates in vitro also increased.
Mol Biol (Mosk)
PMID:[Sea urchin sperm DNP. I. Chemical composition and template properties of DNP]. 56 76

The ability of H5 and H1 histones, purified from immature or mature pigeon erythroid cells, to suppress RNA synthesis in vitro was compared. It was found that H1 histones from both sources as well as histone H5 from bone marrow suppress RNA synthesis to a comparable degree while H5 from the mature erythrocytes exhibits significantly higher suppression efficiency. H5 histone subfractions, differing in phosphate content, also had different ability to restrict the template activity of chromatin: the higher is the phosphorylation level of H5 histone, the weaker is its effect on the transcription.
Mol Biol (Mosk)
PMID:[Role of serine-rich histone (H5) in bird erythrocyte genome inactivation]. 63 79

The interaction of basic oligopeptides--F2aI histone, iridine and salmine protamines synthetic fragments with DNA has been studied by the methods of thermal denaturation, circular dichroism and equilibrium dialysis. All the peptides investigated are albe to stabilize the DNA helix and change its conformation. This ability grows with the increase of a number of basic residues in the peptide molecule and decreases when there is a serin residue on the end. The binding of the peptide with DNA obtains a cooperative character if 4--6 arginine clusters are present in the molecule. The comparison of the binding coefficient with the thermal denaturation data allowed to propose an important role of nonelectrostatic forces on the binding of the peptides to DNA.
Mol Biol (Mosk)
PMID:[Reaction between synthetic fragment of histone F2al and the protamines iridine and salmine with DNA]. 66 28

Biotin deficient rat liver histones showed decreased phosphorylation and methylation, and increased acetylation rates as compared to normal rat liver histones: these alterations may be related to the observed lower stability of the interactions between histones and DNA. The modifications of the metabolic process might be the consequence of an alteration of the synthesis of the enzymes involved in histone phosphorylation, acetylation and methylation mechanisms and are presumably related to a biotin effect upon the synthesis of RNA and proteins.
Mol Biol Rep 1978 Jun 16
PMID:Effect of biotin on phosphorylation, acetylation, methylation of rat liver histones. 68 85

The effect of removal of various protein fractions on the patterns of transcription of the chromatin isolated from rat liver nuclei after cortisone administration has been studied. The RNA synthesized in vitro on the protein-depleted chromatin templates was investigated by competitive hybridization technique with the nuclear RNA synthesized in vivo. Extraction of chromatin with 0.7 M NaCl (removal of histone H1 and a part of loosely bound nonhistone proteins) did not interfere with the synthesis of the hormone-specific RNA population on chromatin templates. However, treatment of chromatin with 1.0 M NaCl fully eliminated the hormone-related pattern of transcription. Electrophoretic analysis demonstrated that the fractional composition of chromatin proteins is changed under the action of cortisone. An additional protein fraction specific for the hormone-activated chromatin with a lower electrophoretic mobility than H1 histone was found by electrophoresis at pH 2.7. Using the method of SDS electrophoresis, the additional subfraction of H1 histone was observed and the amount of protein located between H1 and H3 histones increase as the result of cortisone injection.
Mol Biol (Mosk)
PMID:[Transcription and the composition of chromatin isolated from rat liver cells after cortisone administration]. 68 96

Utilizing male rat liver cells we describe a method for isolating and fractionating chromosomal proteins. About 99% of chromosomal proteins was dissociated using a three step dissociation procedure. DNA was removed by sedimentation and the histone fractions were separated from the non-histone chromosomal proteins by Bio Rex 70 chromatography. The non-histone chromosomal proteins were fractionated by micro-gradient electrophoresis on SDS-polyacrylamide gels, which proved to be superior to the electrophoretic procedures currently in use. The histones were further separated on polyacrylamide-SDS slab gels using a micro-two-dimensional electrophoretic system. The high resolution of these fractionation procedures greatly enhances the possibility of observing small changes in proteins which may play a role in gene regulation.
Mol Biol Rep 1978 Oct 16
PMID:A new high sensitive analytical micro-scale procedure for chromosomal proteins. 73 84

Hen erythrocyte chromatin was digested with staphylococcal nuclease and fractionated by electrophoresis in polyacrylamide gels. Instead of the three bands described for mouse carcinoma chromatin, four main discrete components (MN1, MN2, MN2E and MN3) were resolved in the mononucleosome fraction of erythrocyte chromatin. MN2 contained all five histones and a DNA fragment of 165--180 base pairs. MN2E comprised four nucleosomal histones plus histone H5 (but not H1) and a DNA fragment of 170--190 base pairs. The relatively nuclease resistant MN3 fraction of erythrocyte nucleosomes contained H1 but no H5 histone. A more accurate analysis of the MN2 fraction in mouse carcinoma nucleosomes revealed some additional microheterogeneity depending on the presence of two different subfractions of H1.
Mol Biol Rep 1978 Oct 16
PMID:Separation of nucleosomes containing histones H1 and H5. 73 86

Chromatin subunits ("nucleosomes") isolated from a mild staphylococcal nuclease digest of chromatin by a sucrose gradient centrifugation have been studied. We found that such preparation contains nucleosomes of the two discrete types which can be separated from each other by a low-ionic-strength polyacrylamide gel electrophoresis. Nucleosome of the first type contains all five histones and a DNA fragment 170--180 base pairs long, whereas nucleosome of the second type lacks histone H1 and its DNA fragment is approximately 140 base pairs long. Purified dimer of the nucleosome (dinucleosome) can be fractionated by gel electrophoresis into three discrete bands which correspond to dinucleosomes, containing two, one and no molecules of H1 histone. Similar heterogeneity with respect to the content of histone H1 probably exists in the case of larger oligonucleosomes. These and related findings strongly suggest that the H1 molecule is bound to a short (30--40 base pairs) terminal stretch of the nucleosomal DNA segment which can be removed by nuclease (possibly in the form of H1--DNA complex) without any significant disturbance of the main structural features of the nucleosome.
Mol Biol (Mosk)
PMID:[Structure of chromosomal deoxyribonucleoproteins. IX. Heterogeneity of chromatin subunits in vitro and location of histone H1]. 75 77


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>