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J Biol Chem, Vol. 273, Issue 50, 33443-33448, December 11, 1998
From the Department of Pathology and the Program in Immunology,
Sackler School of Graduate Studies, Tufts University School of
Medicine, Boston, Massachusetts 02111
The transcription factor TFII-I binds to distinct
promoter sequences including an initiator element in several eukaryotic genes. Here we demonstrate that TFII-I is phosphorylated in
vivo at serine/threonine and tyrosine residues in the absence of
any apparent extracellular signals. This "basal" phosphorylation of TFII-I is not required and does not affect its specific DNA binding, but is critical for its in vitro transcriptional properties
via the V
Regulation of TFII-I Activity by Phosphorylation
promoter. To better assess the functional role of
phosphorylation in regulating TFII-I activity, we focused on tyrosine
phosphorylation of TFII-I. Ectopically expressed recombinant TFII-I,
like its native counterpart, exhibits tyrosine phosphorylation in the
absence of distinct extracellular signals. More important, mutation of a potential consensus tyrosine phosphorylation site in TFII-I leads to
severe reduction in its basal transcriptional activation of the V
promoter in vivo. Taken together, these data suggest that
tyrosine phosphorylation of TFII-I is important for its
initiator-dependent transcriptional activity.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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