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J Biol Chem, Vol. 273, Issue 19, 11625-11629, May 8, 1998
From the Department of Biochemistry and Microbiology, University of
Victoria, Victoria, British Columbia V8W 3P6, Canada
We have reconstituted oligonucleosome complexes
containing histone H1 starting from a synthetic DNA template,
consisting of 12 tandemly arranged 208-base pair fragments of the 5 S
rRNA gene, purified HeLa histone octamers, and histone H1. A ratio of
histone H1 per histone octamer used in the reconstitution (0.8-0.9 mol of histone H1/mol of histone octamer) similar to that observed in
vivo was used. The reconstituted chromatin complexes exhibit a
salt-dependent folding, which is almost indistinguishable
from that exhibited by chromatin fragments obtained from nuclease
digestion of native chromatin. The folding of this reconstituted
chromatin complex seems to be rather independent of the symmetrical or
asymmetrical position occupied by H1 in the individual nucleosomes.
Binding of histone H1 to the oligonucleosome complexes, under the
stoichiometric binding conditions used, had no inhibitory effect on the
transcriptional potential of these complexes.
Folding of Chromatin in the Presence of Heterogeneous Histone
H1 Binding to Nucleosomes
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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