Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA.-Reference-Cited by-同舟云学术

Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA.

Published:1993-01 Issue:1 Volume:268 Page:305-314
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hong L.,Schroth G.P.,Matthews H.R.,Yau P.,Bradbury E.M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequences

2. Histone hyperacetylation: its effects on nucleosome conformation and stability

3. Use of selectively trypsinized nucleosome core particles to analyze the role of the histone “tails” in the stabilization of the nucleosome

4. Proteolytic Digestion Studies of Chromatin Core-Histone Structure. Identification of the Limit Peptides of Histones H3 and H4

5. DNA, Chromatin and Chromosomes;Bradbury,1981

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