Dissociation of nucleosomal particles by chemical modification. Equivalence of the two binding sites for H2A. H2B dimers
Treatment of nucleosomal particles with dimethylmaleic anhydride, a reagent for protein amino groups, is accompanied by a biphasic release of histones H2A plus H2B; one H2A.H2B dimer is more easily released than the other. This behavior allows the preparation of nucleosomal particles containing only one H2A.H2B dimer, which were complemented with SVI-labeled H2A.H2B. These reconstituted particles, which contain one labeled and one unlabeled H2A.H2B dimer, were treated with the amount of reagent needed to release one of the two H2A.H2B dimers. Radioactivity was equally distributed between residual particles and released proteins, which is consistent with equivalent binding sites in the nucleosomal particle for H2A.H2B dimers, rather than with intrinsically different sites. The asymmetric release of H2A.H2B dimers would be caused by a change in the binding site of one dimer following the release of the other. This behavior might be related to the structural dynamics of nucleosomes.
- Research Organization:
- Consejo Superior de Investigaciones Cientificas, Madrid, Spain
- OSTI ID:
- 6085888
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 16
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
HISTONES
BIOCHEMISTRY
IODINE 125
TRACER TECHNIQUES
NUCLEOSOMES
MOLECULAR STRUCTURE
CHICKENS
ERYTHROCYTES
ANIMALS
BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BIRDS
BLOOD
BLOOD CELLS
BODY FLUIDS
CHEMISTRY
CHROMATIN
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
FOWL
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MATERIALS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PROTEINS
RADIOISOTOPES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques