Please use this identifier to cite or link to this item:
|Title:||Dissociation of nucleosomal particles by chemical modification. Equivalence of the two binding sites for H2A.H2B dimers|
|Authors:||Jordano, Juan; Nieto, M. Ángela; Palacián, Enrique|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Citation:||Journal of Biological Chemistry 260(16): 9382-9384 (1985)|
|Abstract:||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 125I-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.|
|Description:||3 páginas, 3 figuras.|
|Publisher version (URL):||http://www.jbc.org/content/260/16/9382.abstract|
|Appears in Collections:||(CBM) Artículos|
Files in This Item:
There are no files associated with this item.
Show full item recordCSIC SFX Links
WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.