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(Received for publication, December 11, 1996, and in revised form, February 19, 1997)
From the Department of Biochemistry and Molecular Biology and The
Center for Gene Regulation, The Pennsylvania State University,
University Park, Pennsylvania 16802-4500
To investigate the potential mechanisms by which
the SWI/SNF complex differentially regulates different genes we have
tested whether transcription factors with diverse DNA binding domains were able to exploit nucleosome disruption by SWI/SNF. In addition to
GAL4-VP16, the SWI/SNF complex stimulated nucleosome binding by the
Zn2+ fingers of Sp1, the basic helix-loop-helix
domain of USF, and the rel domain of NF-
B. In each case SWI/SNF
action resulted in the formation of a stable factor-nucleosome complex
that persisted after detachment of SWI/SNF from the nucleosome. Thus,
stimulation of factor binding by SWI/SNF appears to be universal. The
degree of SWI/SNF stimulation of nucleosome binding by a factor appears to be inversely related to the extent that binding is inhibited by the
histone octamer. Cooperative binding of 5 GAL4-VP16 dimers to a 5-site
nucleosome enhanced GAL4 binding relative to a single-site nucleosome,
but this also reduced the degree of stimulation by SWI/SNF. The SWI/SNF
complex increased the affinity of 5 GAL4-VP16 dimers for nucleosomes
equal to that of DNA but no further. Similarly, multimerized NF-B
sites enhanced nucleosome binding by NF-B and reduced the
stimulatory effect of SWI/SNF. Thus, cooperative binding of factors to
nucleosomes is partially redundant with the function of the SWI/SNF
complex.
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