Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histone H1 (F1) in Eukaryote Chromatin

Bradbury, E. Morton; Cary, Peter D.; Chapman, George E.; Crane‐Robinson, Colyn; Danby, Shirley E.; Rattle, H. W. E.; Boublík, M.; Palau, Jaume; Aviles, Francesc X.

doi:10.1111/j.1432-1033.1975.tb04032.x

Cited by 137 publications

(61 citation statements)

References 17 publications

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“…Solubilized linker histones change their tertiary structure, and the charged tails obtain a random coil conformation (72). The final structure of linker histones in vivo is probably achieved only after binding to chromatin (73), and it may not be possible to retrieve completely this structure after reconstitution in vitro.…”

Section: Discussionmentioning

confidence: 99%

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

et al. 2004

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Background:Linker histones constitute a family of lysinerich proteins associated with nucleosome core particles and linker DNA in eukaryotic chromatin. In permeabilized cells, they can be extracted from nuclei by using salt concentration in the range of 0.3 to 0.7 M. Although other nuclear proteins are also extracted at 0.7 M salt, the remaining nucleus represents a template that is relatively intact. Methods: A cytochemical method was used to study the affinity of reconstituted linker histones for chromatin in situ in cultured human fibroblasts. We also investigated their ability to condense chromatin by using DNA-specific osmium ammine staining for electron microscopy. Results: Permeabilized and H1-depleted fibroblast nuclei were suitable for the study of linker histone-chromatin

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Section: Discussionmentioning

confidence: 99%

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

et al. 2004

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“…Related studies on H 1 have already been published [23,24]. Hydrodynamic studies have shown that H 5 does not aggregate at high ionic strength [8,28] and thereby resembles H 1 and not the remaining four histone fractions.…”

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confidence: 96%

“…There is at present no evidence to suggest why H 1 should be replaced in large part by H 5 and the present structural investigation of H 5 was carried out to point out the similarities and differences between H 5 and H 3 . Related studies on H 1 have already been published [23,24].…”

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Structural Studies of Chicken Erythrocyte Histone H5

Crane‐Robinson

Danby

Bradbury

et al. 1976

European Journal of Biochemistry

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Spectroscopic studies (nuclear magnetic resonance, circular dichroism and infrared) have been carried out on chicken erythrocyte histone H 5 and on three peptides cleaved therefrom: 1-31, 32-197 and 58-197. It is shown that at ionic strengths above 0.1M part of the H 5 molecule takes up a globular conformation containing 14% a helix but no p sheet structure. Several details of the circular dichroism and nuclear magnetic resonance spectra indicate that the globular region is located in the N-terminal half of the molecule and this proposal is supported by the observation that the peptide 32-197 is largely incapable of folding and the peptide 59-197 is completely incapable of folding. Structural similarities and differences between histone H 5 and histone H 1 are discussed.The nucleated erythrocytes of birds, reptiles, amphibians and fish contain a very basic histone, H5, that has not been found in other tissues [l -51. H 5 largely, but not completely, replaces H 1 and the two histones are not dissimilar in amino acid composition and molecular weight [4,6 -81. A significant difference between the two histones is that H 5 contains 11 % arginine whilst H 1 contains only 2%. In this respect H 5 resembles the 4 1 histones of marine invertebrate sperm (in particular sea urchins) which totally replace the H I and also contain about 11% arginine in addition to roughly 25% lysine 191. Early observations of the occurrence and composition of H 5 resulted in the suggestion that its function is the total suppression of the genome in the fully mature erythrocyte [lo]. Detailed studies on anemic chickens have subsequently shown, however, that H 5 can be detected even in erythroblasts (when a wide range of protein synthesis is taking place), and does not appear suddenly at the mature erythrocyte stage when protein synthesis is finally terminated [I 1 -151. The function of H 5 in relation to genome suppression is, therefore, not as simple as originally thought. H 5 nevertheless is closely related to H I [I61 and a number of experiments have implicated H 1 in the condensation of diffuse chromatin [17 -191. In particular the state of chromatin is thought to depend on the degree of phosphorylation of H 1 [20,21] and recently it has been shown that H 5 is phosphorylated and dephosphorylated in viuo [22]. There is at present no evidence to Abbreviations. NMR, nuclear magnetic resonance; CD, circular dichroism.suggest why H 1 should be replaced in large part by H 5 and the present structural investigation of H 5 was carried out to point out the similarities and differences between H 5 and H 3 . Related studies on H 1 have already been published [23,24]. Hydrodynamic studies have shown that H 5 does not aggregate at high ionic strength [8,28] and thereby resembles H 1 and not the remaining four histone fractions. The monomeric state of H 1 has led to proposals that its function is quite separate from that of the other histones and this may also be true for H5. In chicken erythrocytes the stoichiometry of histones H 5 and H 1 together, wi...

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“…RP-HPLCpurified histones exhibit a similar spectrum, but the molar ellipticities at 222 and 208 nm have been significantly reduced. Since it is possible to estimate the α-helical contribution to the spectrum from the ellipticity at 222 nm [33], we estimated that the reduction on the ellipticity at 222 nm represents a decrease of 15 % in the overall α-helix context of these histones. These alterations in the secondary structure are most probably responsible for the anomalous association pattern of these histones.…”

Section: Rp-hplc Prevents the Correct Association Of Histones Into A mentioning

confidence: 99%

Reconstitution of native-like nucleosome core particles from reversed-phase-HPLC-fractionated histones

Moore

Rice

Maya

et al. 1997

Biochemical Journal

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We have reconstituted nucleosome core particles from reversed-phase-HPLC-purified chicken erythrocyte core histones and 145 bp random-sequence DNA fragments. Characterization of the resulting nucleoprotein complexes by sedimentation velocity, CD and DNase I footprinting showed that they are structurally indistinguishable from native nucleosome core particles. Furthermore, we have shown that the ability to reproduce these native-like structural features in these reconstituted nucleosome core particles is basically independent of the biological source or the method used (i.e. salt versus acid) for the extraction of histones before their HPLC fractionation. The usefulness and relevance of this approach for the reconstitution of native-like chromatin structures from histone types (histone variants/post-translationally modified histones), which are usually available only in relatively small amounts, is discussed.

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Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histone H1 (F1) in Eukaryote Chromatin

Cited by 137 publications

References 17 publications

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

Structural Studies of Chicken Erythrocyte Histone H5

Reconstitution of native-like nucleosome core particles from reversed-phase-HPLC-fractionated histones

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