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

作者: Marjorie Brand , Ken Yamamoto , Adrien Staub , Laszlo Tora

DOI: 10.1074/JBC.274.26.18285

关键词: TATA-binding proteinTranscription (biology)Multiprotein complexTranscription factorChromatinProtein subunitCell biologyBiologyRNA polymerase IIMolecular biologyNucleosome

摘要: Abstract 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 demonstrate that TFTC, similar other TBP-free TAFII complexes (yeast SAGA, hSTAGA, hPCAF) contains the acetyltransferase hGCN5 acetylate histones in both free nucleosomal context. The recently described TRRAP cofactor for oncogenic factor pathways was also characterized as TFTC subunit. Furthermore, four previously uncharacterized subunits of TFTC: hADA3, hTAFII150, hSPT3, hPAF65β. Thus, polypeptide composition suggests recruited chromatin templates by activators thus may potentiate initiation activation transcription.

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