| First Author | Brand M | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 26 | Pages | 18285-9 |
| PubMed ID | 10373431 | Mgi Jnum | J:320038 |
| Mgi Id | MGI:6867270 | Doi | 10.1074/jbc.274.26.18285 |
| Citation | Brand M, et al. (1999) Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J Biol Chem 274(26):18285-9 |
| abstractText | 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. |
