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The isolation, characterization and partial sequences of the chicken erythrocyte non-histone chromosomal proteins HMG14 and HMG17. Comparison with the homologous calf thymus proteins.

ABSTRACT: Non-histone chromosomal proteins HMG14 and HMG17 were isolated from chicken erythrocyte nuclei. The proteins were characterized by amino acid analysis and by N-terminal sequence analyses. Comparison with the corresponding data for the calf thymus proteins shows that 11% of the residues in HMG14 protein and 5% of the residues in HMG17 protein differ between the two species. Proteins HMG14 and HMG17 therefore do not appear to exhibit the evolutionary stability shown by the nucleosome core histones. Detailed evidence for the amino acid sequence data has been deposited as Supplementary Publication SUP 50101 (4 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. 4. (1978) 169, 5.

SUBMITTER: Walker JM

PROVIDER: S-EPMC1161364 | biostudies-other | 1980 Feb

REPOSITORIES: biostudies-other

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The isolation, characterization and partial sequence of a peptide rich in glutamic acid and aspartic acid (HGA-2 peptide) from calf thymus non-histone chromosomal protein HMG 2. Comparison with a similar peptide (HGA-1 peptide) from calf thymus non-histone chromosomal protein HMG 1.

Project description:A 41-residue peptide (HGA-2) containing a continuous sequence of 35 glutamic and aspartic residues was isolated from non-histone chromosomal protein HMG 2. This highly acidic peptide is compared with a similar peptide (HGA-1) isolated from non-histone chromosomal protein HMG 1.

| S-EPMC1186617 | biostudies-other

The isolation and partial sequence of peptides produced by cyanogen bromide cleavage of calf thymus non-histone chromosomal high-mobility-group protein 2. Sequence homology with non-histone chromosomal high-mobility-group protein 1.

Project description:Peptides produced by CNBr cleavage of non-histone chromosomal protein HMG 2 (CNBr peptides) were isolated and characterized, and their partial sequences were determined. The present sequence data account for over half of the sequence of the protein HMG (high-mobility-group) 2 molecule, and, together with previously published results, provide interesting information on the charge distribution within the molecule. Comparison of the CNBr-peptide-sequence data for protein HMG 2 with the previously published data on the CNBr peptides from protein HMG 1 reveals extensive sequence homology between the two proteins. Detailed evidence for the amino acid-sequence data has been deposited as Supplementary Publication SUP 50095 (6 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1978) 169, 5.

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Interaction of quinacrine mustard with calf thymus histone fractions.

Project description:1. Interactions of histone fractions with quinacrine mustard were investigated by fluorimetry and spectrophotometry and the results were interpreted with the aid of thinlayer chromatography. 2. Characteristic differences were found between the various histone fractions of calf thymus. The conditions that favoured histone conformational changes and aggregation, also favoured interaction between histones and the dye; low concentrations of SO(4) (2-) brought about more interaction than did Cl(-); urea, guanidinium and iodide ions were inhibitory to binding. 3. Changes in the physical state of all the quinacrine mustard-protein complexes occurred as a function of ionic strength and pH. The most salt-dependent interaction was found in the arginine-rich histone fraction. 4. The interaction of the calf thymus histone fractions with quinacrine mustard was compared with the interaction of bovine plasma albumin and protamine with quinacrine mustard. 5. The relationship between dye-binding and the aggregation of histone fractions was discussed.

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Ultracentrifuge tudies of histone fractions from calf thymus deoxyribonucleoprotein.

Project description:Molecular weights and sedimentation coefficients of four major fractions of calf thymus histones were measured. The minimum molecular weights were determined in concentrated solutions of guanidine hydrochloride. The results indicate that, with the possible exception of fraction F3, the fractions are heterogeneous. Comparisons in 0.1m-sodium chloride suggest that fraction F1 does not aggregate and show that fractions F2(a) and F3 aggregate to form larger complexes than does fraction F2(b). The degree of aggregation of each fraction is independent of pH in the range pH1-7. Detailed studies with fraction F2(b) have confirmed that the change in sedimentation coefficient observed as the sodium chloride concentration of the solution is increased results from increases in the apparent molecular weight of the sedimenting units. It has been found that the molecules of fraction F2(b) are present as single molecules only in sodium chloride solutions of 33mm or less. At these low concentrations the effects of charge greatly increase the concentration dependence of the sedimentation rate; the results can, however, be interpreted by using the theory developed by Alexandrowicz & Daniel (1963) and Daniel & Alexandrowicz (1963).

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Analysis of calf thymus histone methylation

Project description:To identify sites of methylated residues, calf thymus histone was analyzed by MALDI-TOF/MS.

2023-04-10 | PXD041342 | JPOST Repository

A study of calf thymus histone fraction F2(b) by gel filtration.

Project description:The gel-filtration behaviour of calf thymus histone fraction F2(b) was studied at three different salt concentrations (0.01m-, 0.10m- and 1.00m-sodium chloride) and two different pH ranges (pH3-4 and pH6.7-7.1). Other histone fractions [F1, F2(a) and F3] were also utilized to assist interpretation of the data. It was found that the Stokes radius of histone fraction F2(b) was not significantly changed when the salt concentration was increased, implying that the aggregation of the individual histone molecules (Edwards & Shooter, 1969) resulted in only relatively minor changes in the hydrodynamic volume. Aggregation would appear to be due to the salting out of hydrophobic regions giving rise, in the aggregate, to a compact core of hydrophobic groups from which protrude the remaining basic parts of the molecule. Repulsion between charged groups on the basic regions of individual histone molecules would give the aggregate approximately spherical symmetry, the diameter of the aggregate approximating to the length of a single histone molecule.

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Studies on the tissue specificity of the high-mobility-group non-histone chromosomal proteins from calf.

Project description:The high-mobility-group (HMG) non-histone chromosomal proteins from calf thymus, liver, spleen and kidney were extracted, and fractionated by CM-Sephadex chromatography and trichloroacetic acid precipitation. The isolated proteins HMG 1, HMG 2 and HMG 17 from the tissues were compared by polyacrylamide-gel electrophoresis, isoelectric focusing and amino acid analysis. The results show that the three proteins are very similar in the tissues studied, implying a lack of tissue specificity.

| S-EPMC1185803 | biostudies-other

HMG (high-mobility-group)-14/17-like proteins in calf thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins.

Project description:Two-dimensional polyacrylamide-gel electrophoresis of acid extracts of thyroid and thymus tissue, and of thyroid nuclei, revealed the presence of three HClO4-soluble nuclear proteins, PS.1, PS.2 and PS.3, whose electrophoretic mobilities closely resembled those of HMG (high-mobility-group) proteins 14 and 17. PS.1 co-migrated with HMG 14 on CM-Sephadex column chromatography. Like HMG 14, PS.2 and PS.3 were phosphorylated in calf thyroid slices; 32P-labelling of PS.3 was stimulated by thyrotropin. Thyrotropin also induced a rapid increase in the labelling of A5, an HMG-14/17-like protein found in whole calf thyroid and thymus tissue, but not in thyroid nuclei.

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Cysteine in calf-thymus histones.

Project description:1. Calf-thymus histones contain cysteine, which is present almost entirely in the arginine-rich fraction F3 to the extent of about 1mole in 15000g. weight of the histone. 2. The cysteine in fraction F3 is readily available to thiol reagents and the protein yields an approximately equivalent amount of cysteic acid on oxidation with performic acid.

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