In Vivo Functions of Histone Acetylation/Deacetylation in Tup1p Repression and Gcn5p Activation

Abstract

Histone acetylation is a dynamic process that affectschromatin structure and transcriptional regulation at multiple levels. Acetylation occurs exclusively on lysineresidues in the amino-terminal "tails" of the core histones(Turner 1991; Wade et al. 1997). Since these tail domainsare external to the core particle, they are in a unique position to affect DNA-histone interactions, nucleosome-nucleosome interactions, and interactions between nonhistone regulatory factors and the histones (Hansen 1997;Luger et al. 1997). Acetylation could easily influence anyof these interactions by changing the charge and the structure of the histone tails...