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(Received for publication, May 2, 1996, and in revised form, August 23, 1996)
From the Laboratory of Gene Regulation, The Picower Institute for
Medical Research, Manhasset, New York 11030
NF-Y is a heterotrimeric transcription factor
that specifically recognizes a CCAAT box motif found in a variety of
eukaryotic promoter and enhancer elements. The subunit association and
DNA binding properties of the NF-Y complex were examined as a function of redox state using recombinant NF-YA, NF-YB, and NF-YC subunits. Reduction of NF-YB by dithiothreitol (DTT) was essential for
reconstitution of specific NF-Y CCAAT box DNA binding activity in
vitro. Approximately 30% of the Escherichia
coli-derived NF-YB subunit existed as intermolecular disulfide-linked dimers. NF-YB mutants in which the highly conserved cysteine residues at positions 85 and 89 had been converted to serines
existed only as monomers and did not require DTT for functional NF-Y
DNA binding activity. DTT was required, however, for the functional
association of NF-YC with wild-type NF-YB but not with the NF-YB
cysteine mutants. The cellular redox factors Ref-1 and adult T-cell
leukemia-derived factor stimulated the DNA binding activity of
recombinant NF-Y in the absence of DTT. Cells treated with
1-chloro-2,4-dinitrobenzene, an irreversible inhibitor of thioredoxin
reductase, exhibited reduced endogenous NF-Y DNA binding activity.
Together these results suggest that the cellular redox environment of
mammalian cells is an important posttranscriptional regulator of NF-Y
subunit association and DNA binding activities.
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28784-28791
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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