Histone-like TAFs within the PCAF histone acetylase complex - PubMed (original) (raw)

Comparative Study

. 1998 Jul 10;94(1):35-44.

doi: 10.1016/s0092-8674(00)81219-2.

Affiliations

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

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Comparative Study

Histone-like TAFs within the PCAF histone acetylase complex

V V Ogryzko et al. Cell. 1998.

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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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Comment in

• The TAFs in the HAT.
  Struhl K, Moqtaderi Z. Struhl K, et al. Cell. 1998 Jul 10;94(1):1-4. doi: 10.1016/s0092-8674(00)81213-1. Cell. 1998. PMID: 9674419 Review. No abstract available.

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