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J Biol Chem, Vol. 274, Issue 26, 18285-18289, June 25, 1999

Identification of TATA-binding Protein-free TAFII-containing Complex Subunits Suggests a Role in Nucleosome Acetylation and Signal Transduction

Marjorie Brand, Ken Yamamoto, Adrien Staub, and Laszlo Tora

From the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/Université Louis Pasteur BP 163-67404 Illkirch Cedex, CU de Strasbourg, France

Recently we identified a novel human (h) multiprotein complex, called TATA-binding protein (TBP)-free TAFII-containing complex (TFTC), which is able to nucleate RNA polymerase II transcription and can mediate transcriptional activation. Here we demonstrate that TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. The recently described TRRAP cofactor for oncogenic transcription factor pathways was also characterized as a TFTC subunit. Furthermore, we identified four other previously uncharacterized subunits of TFTC: hADA3, hTAFII150, hSPT3, and hPAF65beta . Thus, the polypeptide composition of TFTC suggests that TFTC is recruited to chromatin templates by activators to acetylate histones and thus may potentiate initiation and activation of transcription.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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