Histone-like TAFs within the PCAF Histone Acetylase Complex

• Published in: Cell Vol. 94; no. 1; pp. 35 - 44
• Main Authors: Ogryzko, Vasily V, Kotani, Tomohiro, Zhang, Xiaolong, Schiltz, R.Louis, Howard, Tazuko, Yang, Xiang-Jiao, Howard, Bruce H, Qin, Jun, Nakatani, Yoshihiro
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10-07-1998
• Subjects: Acetyltransferases - chemistry; Amino Acid Sequence; DNA-Binding Proteins - isolation & purification; Fungal Proteins; HeLa Cells; Histone Acetyltransferases; Histones - isolation & purification; Humans; Macromolecular Substances; Mass Spectrometry; Molecular Sequence Data; Nuclear Proteins - isolation & purification; Protein Kinases; Saccharomyces cerevisiae Proteins; Sequence Analysis; Sequence Homology, Amino Acid; Transcription Factors - isolation & purification
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(00)81219-2

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
II31 and hTAF
II20/15, respectively. The PCAF complex has a novel histone H4–like subunit with similarity to hTAF
II80 that interacts with the histone H3–like domain of hTAF
II31. Moreover, the PCAF complex has a novel subunit with WD40 repeats having a similarity to hTAF
II100.