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(Received for publication, October 10,
1995; and in revised form, December 6, 1995) The nucleosome is the fundamental component of the eukaryotic
chromosome, participating in the packaging of DNA and in the regulation
of gene expression. Its numerous interactions imply a structural
dynamism. Previous biophysical studies under limited sets of conditions
have not been able to reconcile structural differences and transitions
observed. We have determined a series of nucleosome conformations over
a >10,000-fold range in salt concentration using a combination of
biochemical methods, spectroscopic electron microscopy, and
three-dimensional reconstruction techniques for randomly oriented
single particles. This study indicates several ionic strength-dependent
nucleosome conformations and also reconciles the differences between
currently existing divergent models for the nucleosome. At low ionic
environments, the particle appears highly elongated, becoming more
compact and prolate ellipsoidal as ionic strength is increased to 10
mM NaCl. At 30 mM NaCl, the particle exhibits a
spheroidal conformation. As ionic strength is increased to 150 mM NaCl, the nucleosome conformation changes and becomes oblate.
Above 450 mM NaCl, the structure becomes highly elongated
again. The result of this study is a unifying concept in which the
three-dimensional structure of the nucleosome is inferred to be dynamic
in response to ionic interactions and in accord with biochemical and
genetic studies.
Volume 271,
Number 7,
Issue of February 16, 1996 pp. 3677-3683
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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