Literature DB >> 9674425

Histone-like TAFs within the PCAF histone acetylase complex.

V V Ogryzko1, T Kotani, X Zhang, R L Schiltz, T Howard, X J Yang, B H Howard, J Qin, Y Nakatani.   

Abstract

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.

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Year:  1998        PMID: 9674425     DOI: 10.1016/s0092-8674(00)81219-2

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  174 in total

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Journal:  Mol Cell Biol       Date:  2000-01       Impact factor: 4.272

Review 7.  Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms.

Authors:  M E Massari; C Murre
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Journal:  Mol Cell Biol       Date:  2001-03       Impact factor: 4.272

9.  Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis.

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Journal:  Mol Cell Biol       Date:  2002-03       Impact factor: 4.272

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