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J. Biol. Chem., Vol. 277, Issue 7, 4853-4858, February 15, 2002
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From the Department of Biochemistry and Biophysics, Texas A&M
University, College Station, Texas 77843-2128
Many small nuclear RNA gene promoters are
activated by SphI postoctamer homology (SPH)-binding
factor/selenocysteine tRNA gene transcription activating factor
(SBF/Staf). Whereas this transcription factor was initially identified
by its ability to bind to SPH elements in such promoters, it was more
recently shown to have the capacity to activate transcription of a
synthetic mRNA gene promoter through a distinct activation domain.
Here, we show that the human interferon regulatory factor-3
(IRF-3) gene promoter contains a functional SPH element
that is bound by SBF/Staf in vitro and in transfected cells.
To whom correspondence should be addressed: Dept. of
Biochemistry and Biophysics, Texas A&M University, 2128 TAMU,
College Station, TX 77843-2128.
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