Open AccessAggregation of small oligonucleosomal chains into 300-A globular particles.
Author(s) -
José L. Jorcano,
G. Meyer,
Loren A. Day,
Manfred Renz
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.11.6443
Subject(s) - micrococcal nuclease , globular protein , biophysics , chemistry , ionic strength , particle (ecology) , particle size , nucleosome , lysine , chromatin , crystallography , biochemistry , biology , dna , amino acid , aqueous solution , organic chemistry , ecology
Chicken erythrocyte oligonucleosomes (trimers to about 20-mers) are able to interact with each other through the very lysine-rich histones (H1 and H5) and form heterogeneous globular particles with a mean diameter of about 300 A. These particles assemble spontaneously during micrococcal nuclease digestion of chromatin in the presence of 30 mM NaCl and contain approximately 25 nucleosomes. They are sensitive to ionic strength and unfold at lower salt concentrations but can be reconstituted by restoring the initial salt concentration. Even at 30 mM NaCl, the particles remain dynamic structures, being in equilibrium with their oligonucleosomal components as revealed by the fact that particle stability depends on the concentration of oligonucleosomes.