Non-histone chromosomal proteins. Evidence for their role in mediating the binding of histones to deoxyribonucleic acid during the cell cycle

Stein, Gary S.; Hunter, G.; Lavie, Lena

doi:10.1042/bj1390071

Cited by 30 publications

(9 citation statements)

References 42 publications

(50 reference statements)

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“…Common to all the models is the supposition that binding involves several different modes of interaction and that for highly specific recognition to occur, a protein has to envelope the DNA in one of its cavities or has to be enveloped by the DNA in one of the grooves. Since non-histone chromosomal proteins are largely regarded as being involved in the regulation of gene expression [21][22][23][24][25] a close fit for their binding to DNA is required. Intercalating agents are therefore likely to interfere with their binding.…”

Section: Discussionmentioning

confidence: 99%

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Jost

Clark

1975

FEBS Letters

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Section: Discussionmentioning

confidence: 99%

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Jost

Clark

1975

FEBS Letters

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“…The first hypothesis of the probable mechanism of NHP action suggested, that negatively charged NHP may interact with positively charged histones thereby, unmasking selected regions of DNA for transcription (5,6,7). Furthermore, interactions of NHP with specific DNAsequences were described (8)(9)(10)(11)(12)(13).…”

Section: Introductionmentioning

confidence: 97%

Incorporation of various amino acids into non-histone chromatin protein fractions of spleen cells of mice immunized with IgG

Rakowicz-Szulczynska

Horst

1981

Mol Cell Biochem

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Incorporation of three various amino acids ([3H]-tryptophan, [3H]-methionine or [3H]-leucine) into the non-histone chromatin proteins, synthesized in spleen cells of mice after immunization with IgG, is described. Two new fractions of non-histone chromatin proteins (I-mol. wt. below 3 000 and B1-mol. wt. about 120 000), appearing during the immune reaction were labelled with [3H]-tryptophan and [3H]-methionine but not with [3H]-leucine. Synthesis of these fractions was observed only at the time of maximal RNA synthesis. A suggestion about the role of tryptophan and methionine in non-histone chromatin proteins in the regulatory processes of gene activation is discussed on the basis of their selective binding to DNA.

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“…The change of the strength of histone binding to DNA at different stages of the cell cycle has also been demonstrated [25]. Moreover during the transition from one stage to another, some histone fractions strengthen, and others weaken their bonds with DNA [26].…”

mentioning

confidence: 93%

“…Disruption of histone-histone interactions within chromatin by concentrated urea or detergents makes histone H1 the last in the order of dissociation induced by the increases in the ionic strength of the medium [7,9,10,12,15,25]. At a certain concentration of urea the order of histone dissociation by salt is the following: H2B+H2A, H1, H3+H4 [9].…”

Section: Histone-histone Interaction Induced Bymentioning

confidence: 99%

“…In the presence of urea and of detergents destroying non-ionic interactions and simultaneously the histone complexes, histone H 1 binds to DNA more strongly than other histones [7,9,10,12,15,19,25]. In the absence of agents mentioned above the lowering of salt concentration in water/salt solutions promotes the disassembly of histone complexes [39,40,44 -471.…”

Section: The Order Of Histone Removal F R O M Water Solution By Titramentioning

confidence: 99%

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On Mechanisms Determining the Interrelationships between DNA and Histone Components of Chromatin

Paponov

Gromov

Sokolov

et al. 1980

European Journal of Biochemistry

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The relative affinity of histones for DNA was studied by the analysis of competitive histone binding to DNA in whole histone/DNA mixtures at physiological and low ionic strengths as well as in water. Use of polyphosphate in similar experiments, as a model of DNA deprived of hydrophobic functional groups allowed us to reject the hypothesis that hydrophobic DNA-histone interaction plays a decisive role in the determination of the relative affinity of histones for DNA, because the orders of histone preference for DNA and for polyphosphate were the same. The relative histone affinity for DNA does not depend on the secondary structure of DNA or on the ionic strength of salt solutions, though the differences in the histone affinities for DNA decrease on lowering the salt concentration. The binding orders of the first and the last molecules of histone type to DNA, studied at various DNA/histone ratios in the medium of physiological ionic strength, are the following: H3+H4, H2A+H2B, H1 and H3+H4, H2A, H2B, H1. In water the binding orders of the first and the last histone molecules to DNA are identical : H 3 + H 4, H 2A, H 2 B + H 1. It is concluded that the relative histone affinity for DNA in water/salt solutions is determined by non-ionic interactions between histones bound to DNA. The folding of DNA induced by histone-histone interaction seems to lead to the increase in the correlation between amino acid residues in the histone regions bound to DNA and the ionic DNA-histone interaction becoming stronger.Since the appearance of the hypothesis about the repressive role of histones in chromosomes [l], for over a quarter of a century DNA-histone interactions have been a matter of steady interest to researchers studying the mechanisms of gene regulation in eucaryotic cells. The discovery of chemical heterogeneity of the histone component of chromatin has made it necessary to explore separate histone fraction affinities for DNA, because the principle of the biological molecule affinity lies at the foundation of all living processes [2] and determines biological specificity [3]. The histone affinity for DNA has been studied in two principal ways : (a) by investigation of DNA-histone complex decomposition, i. e. of histone dissociation from DNA, by modification of the medium into which the extracted chromatin is inserted [4-171; and (b) investigation of DNA-histone complex formation in the mixtures of DNA and whole histone [9,18,19] molecules without change in their charges, alterations (near neutral pH) of ionic strength and ionic composition of solvent [4-6,8,9,13 -15,18,20-221, addition of urea [7 -9,191, of alcohols [8,23,24], and of neutral detergents [13,14] to water/salt solutions; (b) the modifications leading to variation in the electrostatic charges of interacting components, addition of ionic detergents to water/salt solutions [lo-12,15,25], acid titration [16], alkaline titration [17].By now essential differences have been found both in the strength of histone fraction binding to DNA, and in the influence o...

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Non-histone chromosomal proteins. Evidence for their role in mediating the binding of histones to deoxyribonucleic acid during the cell cycle

Cited by 30 publications

References 42 publications

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Incorporation of various amino acids into non-histone chromatin protein fractions of spleen cells of mice immunized with IgG

On Mechanisms Determining the Interrelationships between DNA and Histone Components of Chromatin

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