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

• Published in: The Journal of biological chemistry Vol. 274; no. 26; pp. 18285 - 18289
• Main Authors: Brand, M, Yamamoto, K, Staub, A, Tora, L
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 25.06.1999
• Subjects: Acetylation; Acetyltransferases - metabolism; Carrier Proteins - metabolism; Cell Cycle Proteins; DNA-Binding Proteins - metabolism; Histone Acetyltransferases; Humans; Macromolecular Substances; Multiprotein Complexes; Nucleosomes - metabolism; p300-CBP Transcription Factors; RNA Polymerase II - metabolism; Saccharomyces cerevisiae Proteins; Signal Transduction; TATA-Binding Protein Associated Factors; TATA-Box Binding Protein; Trans-Activators - metabolism; Transcription Factor TFIID; Transcription Factors - metabolism; Transcription Factors - physiology; Transcription Factors, TFII - physiology; Transcriptional Activation
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.26.18285

Recently we identified a novel human (h) multiprotein complex, called TATA-binding protein (TBP)-free TAF II -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 TAF II 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, hTAF II 150, hSPT3, and hPAF65β. 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.