SAGA HAT complex

Histone acetyltransferases also form large complexes that acetylate not only histones but also other nuclear proteins.281-283 The SAGA HAT complex of S. cerevisiae has a molecular mass of 2.0 MDa and contains at least 14 subunits.2833 Large acetylating complexes have also been identified in Tetrahymena, Drosophila, Arabidopsis, and mammalian species.283 Some subunits of these complexes have been identified as previously known transcription factors. Such multiprotein complexes are sometimes described as cis-regulatory elements (CREs).283b/C... 

Histone acetyltransferases also form large complexes that acetylate not only histones but also other nuclear proteins. The SAGA HAT complex of... 

Fig. 1. Possible subunit structure of TFIID. On the basis of immuno-EM studies (Leurent et al., 2002), yeast two-hybrid data (Andel et al., 1999 Brand et al., 1999 Yatherajam et al., 2003), and in vitro protein interaction data (see text), a model of TFIID interactions was constructed. TAFs that appear in both TFIID and the SAGA HAT complex are shaded. BD1 and BD2 signify the bromodomains found in higher eukaryotic TAF1 or in yeast Bdfl. The exact stoichiometry of histone-like TAFs within each lobe is unclear some data indicate an octamer-like structure, whereas others support two tetramers.

B. SAGA HAT Complex Consists of Modular Functional Domains. 185... 

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