Nucleic Acids Research, Vol 27, Issue 2 517-525, Copyright © 1999 by Oxford University Press
P Blomquist, S Belikov and O Wrange
The organization of DNA into chromatin is important in the regulation of
transcription, by influencing the access of transcription factors to their
DNA binding sites. Nuclear factor 1 (NF-1) is a transcription factor which
binds to DNA constitutively and which interacts with its cognate DNA site
with high affinity. However, this affinity is drastically reduced,
approximately 100- to 300-fold, when the binding site is organized into a
nucleosome. Here we demonstrate that the introduction of stretches of
adenines of length 5 nt (A-tracts) on both sides of the NF-1 binding site
has a distinct effect on NF-1 binding to a nucleosomal, but not to a free,
NF-1 binding site. The position of the A-tracts, relative to the rotational
phase of a synthetic DNA bending sequence, the TG-motif, decides whether
the NF-1 affinity increases or decreases. The NF-1 binding affinity is
seven times stronger when the flanking A-tracts are positioned out-of-phase
with the TG-motif than it is when the A-tracts are positioned in-phase with
the TG-motif. We demonstrate that this effect correlates with differences
in DNA curvature and apparent histone octamer affinity. We conclude that
DNA curvature influences the local histone-DNA contacts and hence the
accessibility of the NF-1 site in a nucleosome context.
ARTICLES
Increased nuclear factor 1 binding to its nucleosomal site mediated by sequence-dependent DNA structure
Laboratory of Molecular Genetics, Department of Cell and Molecular Biology, Medical Nobel Institute,Karolinska Institute, S-171 77 Stockholm, Sweden.
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