作者: Marjorie Brand , Ken Yamamoto , Adrien Staub , Laszlo Tora
关键词: TATA-binding protein 、 Transcription (biology) 、 Multiprotein complex 、 Transcription factor 、 Chromatin 、 Protein subunit 、 Cell biology 、 Biology 、 RNA polymerase II 、 Molecular biology 、 Nucleosome
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.