Nucleic Acids Research, Vol 24, Issue 2 321-329, Copyright © 1996 by Oxford University Press
DP Bazett-Jones, E Mendez, GJ Czarnota, FP Ottensmeyer and VG Allfrey
We have characterized the structure of transcriptionally active nucleosome
subunits using electron spectroscopic imaging. Individual nucleosomes were
analyzed in terms of total mass, DNA and protein content, while the
ensemble of images of active nucleosomes was used to calculate a
three-dimensional reconstruction. Transcriptionally active nucleosomes were
separated from inactive nucleosomes by mercury- affinity chromatography
thus making it possible to compare their structures. The chromatographic
results combined with electron spectroscopic imaging confirm that active
nucleosomes unfold to form extended U-shaped particles. Phosphorus mapping
indicated that the nucleosomal DNA also underwent a conformational change
consistent with particle unfolding. The three-dimensional structure of the
Hg-affinity purified nucleosomes determined using quaternion-assisted
angular reconstitution methods unites and resolves the different electron
microscopic views of the particle and is concordant with a sulphydryl-
exposing disruption of the H3-H4 tetramer.
ARTICLES
Visualization and analysis of unfolded nucleosomes associated with transcribing chromatin
Department of Anatomy, University of Calgary, Canada.
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