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Literature DB >> 7433099

The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei.

Abstract

The binding curves of histones H1 and H5 to chromatin in nuclei have been determined by a novel method which utilises the differential properties of free and bound histones on cross-linking with formaldehyde. The dissociation is thermodynamically reversible as a function of [NaCl]. The binding curves are independent of temperature over the range 4 degrees - 37 degrees C and independent of pH over the range 5.0 to 9.0. The curves are sigmoid, indicating co-operative dissociation with NaCl. The standard free energy of dissociation in 1 M NaCl for H1 is 0.5 Kcals/mole and for H5 is 3.5 Kcals/mole.

Entities: Chemical Species

Mesh：

Substances：
Chromatin
Histones

Year: 1980 PMID： 7433099 PMCID： PMC324173 DOI： 10.1093/nar/8.16.3535

Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971

26 in total

1. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. Histone H1 in chromatin and in H1 - DNA complexes.

Authors: E M Bradbury; S E Danby; H W Rattle; V Giancotti
Journal: Eur J Biochem Date: 1975-09-01

7. Replacement of histone H1 by H5 in vivo does not change the nucleosome repeat length of chromatin but increases its stability.

Authors: J M Sun; Z Ali; R Lurz; A Ruiz-Carrillo
Journal: EMBO J Date: 1990-05 Impact factor: 11.598

7 in total

The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei.

1. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. Histone H1 in chromatin and in H1 - DNA complexes.

2. Covalent cross-linking of histones in chromatin.

3. Physical studies of isolated eucaryotic nuclei.

4. Selective dissociation of histones from calf thymus nucleoprotein.

5. Dissection of chromosome structure with trypsin and nucleases.

6. The modification of deoxyribonucleohistone by trypsin and chymotrypsin.

7. Protein-nucleic acid interactions. 3. Cation effect on binding strength and specificity.

8. [NaCl dissociation of the nucleoproteins of chicken erythrocytes].

9. Conformational changes associated with f-1 histone-deoxyribonucleic acid complexes. Circular dichroism studies.

10. The partial dissociation of nucleohistone by salts. Hydrodynamic and denaturation studies.

1. Structure analysis of purified histone H5 and of H5 in nuclei by limited proteolysis.

2. Chromatosomes are not produced from Tetrahymena chromatin by micrococcal nuclease digestion.

3. Modification of the lysine residues of histones H1 and H5: effects on structure and on the binding to chromatin.

4. Transcriptional activation of Xenopus class III genes in chromatin isolated from sperm and somatic nuclei.

5. Cell-cycle-dependent dissociation of histone H1 from chromatin in nuclei of P. polycephalum.

6. Selective radiolabelling and identification of a strong nucleosome binding site on the globular domain of histone H5.

7. Replacement of histone H1 by H5 in vivo does not change the nucleosome repeat length of chromatin but increases its stability.