Histone Deacetylase Directs the Dominant Silencing of Transcription in Chromatin: Association with MeCP2 and the Mi-2 Chromodomain SWI/SNF ATPase
This extract was created in the absence of an abstract.
Excerpt
Histone acetylation is intimately connected to transcriptional regulation (Brownell and Allis 1996; Wolffe 1996;Wolffe and Pruss 1996; Grunstein 1997). Acetylation ofthe core histone amino-terminal tails provides a means bywhich transcription factors can gain access to their recognition elements within nucleosomes (Lee et al. 1993;Wolffe et al. 1993; Vettese-Dadey et al. 1996). In addition, acetylation facilitates transcription from nucleosomal arrays (Ura et al. 1997; Nightingale et al. 1998; Tseet al. 1998). Coactivator complexes that function as histone acetyltransferases are required for transcription activation (Brownell et al. 1996; Ogryzko et al. 1996; Yang etal. 1996; Kuo et al. 1998), whereas corepressors containing histone deacetylases confer transcriptional repression(Taunton et al. 1996; Alland et al. 1997; Hassig et al.1997, 1998; Nagy et al. 1997; Wong et al. 1998; D. Vermaak et al., in prep.). Histones are locally modified ontarget promoters (Kuo et al. 1998; Rundlett et al. 1998)and specific lysines in particular histones are functionaltargets for acetyltransferases and deacetylases (Rundlettet al. 1998; Zhang et al. 1998). Histone acetylation statesare dynamic, with acetylated lysines in hyperacetylatedhistones turning over rapidly in transcriptionally activechromatin, but much less rapidly in the hypoacetylatedhistones of transcriptionally silent regions (Covault andChalkley 1980; Zhang and Nelson 1988). The dynamicsof histone acetylation might provide a mechanistic foundation for the reversible activation and repression of transcription (Wade et al. 1997; Wolffe 1997)...
