First Author | Ogryzko VV | Year | 1998 |
Journal | Cell | Volume | 94 |
Issue | 1 | Pages | 35-44 |
PubMed ID | 9674425 | Mgi Jnum | J:320277 |
Mgi Id | MGI:6870978 | Doi | 10.1016/s0092-8674(00)81219-2 |
Citation | Ogryzko VV, et al. (1998) Histone-like TAFs within the PCAF histone acetylase complex. Cell 94(1):35-44 |
abstractText | PCAF histone acetylase plays a role in regulation of transcription, cell cycle progression, and differentiation. Here, we show that PCAF is found in a complex consisting of more than 20 distinct polypeptides. Strikingly, some polypeptides are identical to TBP-associated factors (TAFs), which are subunits of TFIID. Like TFIID, histone fold-containing factors are present within the PCAF complex. The histone H3- and H2B-like subunits within the PCAF complex are identical to those within TFIID, namely, hTAF(II)31 and hTAF(II)20/15, respectively. The PCAF complex has a novel histone H4-like subunit with similarity to hTAF(II)80 that interacts with the histone H3-like domain of hTAF(II)31. Moreover, the PCAF complex has a novel subunit with WD40 repeats having a similarity to hTAF(II)100. |