Structural complementarity in chromatin subunits

Ohlenbusch, Heiko H.

doi:10.1007/bf00366027

Cited by 4 publications

(13 citation statements)

References 3 publications

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“…Since in the Ac3H4 used for 942 Detection of histone acetylation-nduced chromatin changes reconstitution the lysines are modified at positions 5, 12, and 16 (Wouters-Tyrou et al, 1981), the resulting local decrease in positive charge probably induces in the core particle a conformational change that sterically hinders the binding of IRGERA antibodies. This result is consistent with the core particle model of Ohlenbusch (1979Ohlenbusch ( , 1981 that is based on an antiparallel alignment of histone homodimers and in which the N-terminal region of H4 and the C-terminal part of H3 are close neighbours. The fact that the reactivity of IRGERA antibodies was not affected when both mono-acetylated H3 and H4 were incorporated into core particles also supports this model, since it proposes that the acetylated N-terminal regions of H3 and H4 are at opposite ends of the particle (Ohlenbusch, 1981).…”

Section: Discussionsupporting

confidence: 90%

Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation.

Muller¹,

Erard²,

Burggraf³

et al. 1982

The EMBO Journal

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Native, reassociated, and reconstituted core particles from chicken erythrocytes were compared by both biophysical and immunochemical methods. No significant difference between the three types of core particles could be demonstrated by electron microscopy, circular dichroism, or immunochemical analysis with antisera to histone H2B, H2A, and H3. Core particles were also reconstituted with calf thymus non‐acetylated H3, H2A, and H2B with either mono‐, di‐, or tri‐acetylated H4 isolated from cuttle ‐fish testes. The hyperacetylation of H4 did not significantly alter the biophysical characteristics of core particles but it induced several changes in their immunochemical reactivity. Binding to core particles of antibodies specific for H2A, H3, and for the IRGERA (synthetic C‐terminal) peptide of H3 was considerably decreased when di‐ or tri‐acetylated H4 was used for reconstitution, whereas binding of H2B antibodies remained the same. Our results suggest that the presence of hyperacetylated H4 within core particles leads to conformational changes that alter the antigenic determinants of several of the histones present at the surface of chromatin subunits. Since histone acetylation is correlated with the open structure of active chromatin, it may become possible to monitor the activity of chromatin by immunochemical methods.

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Section: Discussionsupporting

confidence: 90%

Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation.

Muller¹,

Erard²,

Burggraf³

et al. 1982

The EMBO Journal

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“…The results described here agree with observations made by other techniques on native nucleosomes, chromatin, or reconstituted nucleosomes (Stratling, 1979;Bottger et al, 1979;Dieterich et al, 1979;Stacks & Schumaker, 1979). The precise arrangement of histones in the core particle is not known, but several models of the nucleosome structure have been proposed (Ohlenbusch, 1979;Trifonov, 1978;Weintraub et al, 1976;Finch & Klug, 1977;Mirzabckov et al, 1978). In two models, it has been suggested that the nucleosome could take an extended conformation by dissociation of the histone octamer into heterotypic tetramers H2j,H2bH3H4 (Weintraub et al, 1976;Mirzabekov et al, 1978).…”

Section: Discussionmentioning

confidence: 99%

Conformation of nucleosome core particles and chromatin in high salt concentration

Wilhelm¹,

Wilhelm²

1980

Biochemistry

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The conformation of nucleosome core particles and chromatin under different ionic strength conditions has been studied by electron microscopic, hydrodynamic, and spectroscopic techniques. In the range of ionic strength used (6--600 mM), all four core histones were bound to the DNA. The sedimentation coefficient of the core particle decreases from 11.3 in 6 mM NaCl to 9.4 in 600 mM NaCl, and an alteration of the circular dichroic spectrum was observed when the ionic strength was increased. Direct evidence for the alteration of the chromatin structure in high salt was obtained by electron microscopy where a very extended conformation of the nucleosome was observed. The protein cross-linking agent dimethylsuberimidate was used to study the histone--histone proximities in the core particles; our experiments reveal that the same histones are in contact in the extended particles and in the compact native particles.

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“…From the known histone-histone interactions revealed in chemical cross-linking studies, a model was suggested which, among other features, placed the two H3 molecules in contact, close to the exit point of the DNA strands and in a fairly accessible position (Klug et al, 1980). This position of H3 agrees with the antiparallel alignment of histone homodimers proposed by Ohlenbusch (1979Ohlenbusch ( , 1981. Immunochemical methods represent a particularly specific procedure for determining which areas of histone molecules are exposed at the surface of nucleosomes.…”

Section: Discussionmentioning

confidence: 61%

Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits.

Muller¹,

Himmelspach²,

Regenmortel³

1982

The EMBO Journal

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The C‐terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130‐135) corresponding to the sequence Ile‐Arg‐Gly‐Glu‐Arg‐Ala (IRGERA) was prepared by solid‐phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits. The antigenic activity of the synthetic peptide IRGERA was found to be very similar to that of the natural CN3 fragment (residues 121‐135), and it inhibited the H3‐anti H3 reaction in complement fixation, solid‐phase radioimmunoassay, and enzyme‐linked immunosorbent assay. Antibodies induced by IRGERA were found to bind equally well to IRGERA coupled to hemocyanin, to the intact H3 molecule, and to chromatin subunits (nucleosomes and core particles). The results demonstrate that the C‐terminal hexapeptide of histone H3 is located at the surface of chromatin subunits and agree with current models proposed for the spatial organization of the chromatin core particle.

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Structural complementarity in chromatin subunits

Cited by 4 publications

References 3 publications

Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation.

Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation.

Conformation of nucleosome core particles and chromatin in high salt concentration

Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits.

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