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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Histone-like TAFs within the PCAF histone acetylase complex.

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.[1]

References

  1. Histone-like TAFs within the PCAF histone acetylase complex. Ogryzko, V.V., Kotani, T., Zhang, X., Schiltz, R.L., Howard, T., Yang, X.J., Howard, B.H., Qin, J., Nakatani, Y. Cell (1998) [Pubmed]
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