Histone-like TAFs within the PCAF histone acetylase complex
Autor: | Xiang Jiao Yang, R. Louis Schiltz, Xiaolong Zhang, Tomohiro Kotani, Yoshihiro Nakatani, Tazuko Howard, Jun Qin, Vasily Ogryzko, Bruce H. Howard |
---|---|
Rok vydání: | 1998 |
Předmět: |
Saccharomyces cerevisiae Proteins
Macromolecular Substances Protein subunit genetic processes Molecular Sequence Data General Biochemistry Genetics and Molecular Biology Mass Spectrometry Fungal Proteins Histones Histone H3 Acetyltransferases Humans Amino Acid Sequence Histone Acetyltransferases TATA-Binding Protein Associated Factors biology Sequence Homology Amino Acid Biochemistry Genetics and Molecular Biology(all) Nuclear Proteins Molecular biology Cell biology SAGA complex DNA-Binding Proteins Histone PCAF PCAF complex biology.protein Transcription factor II D Protein Kinases Sequence Analysis HeLa Cells Transcription Factors |
Zdroj: | Cell. 94(1) |
ISSN: | 0092-8674 |
Popis: | 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. |
Databáze: | OpenAIRE |
Externí odkaz: |