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Preparative separation of nucleosome core particles containing defined‐sequence DNA in multiple translational phases
Author(s) -
Harp Joel M.,
Palmer Elise L.,
York Melissa H.,
Gewiess Andreas,
Davis Matthew,
Bunick Gerard J.
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601305
Subject(s) - histone octamer , nucleosome , histone , linker dna , chromatosome , dna , histone h1 , histone code , biophysics , chemistry , crystallography , biology , genetics
The nucleosome core particle is composed of an octamer of core histone proteins and about 146 bp of DNA. When reconstituted from purified histone octamer and defined‐sequence, nucleosome positioning DNA fragments, the DNA will bind to the histone core in a number of translational phases with respect to the dyad symmetry axis of the histone octamer. Only one of these phases contains symmetrically bound DNA, and it is this species which is required for crystallization and X‐ray diffraction studies. We have developed a technique for separating nucleosome core particles, containing defined‐sequence 146 bp DNA, which differ only in translational phasing of the DNA with respect to the histone octamer core.