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J Biol Chem, Vol. 273, Issue 50, 33443-33448, December 11, 1998

Regulation of TFII-I Activity by Phosphorylation

Carl D. Novina, Venugopalan Cheriyath, and Ananda L. Roy

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 Vbeta 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 Vbeta 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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