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

  1. D.G. EDMONDSON,
  2. W. ZHANG,
  3. A. WATSON,
  4. W. XU,
  5. J.R. BONE,
  6. Y. YU,
  7. D. STILLMAN, and
  8. S.Y. ROTH
  1. *Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030; Division of Molecular Biology and Genetics, Department of Oncological Sciences, University of Utah Health Science Center, Salt Lake City, Utah 84132

This extract was created in the absence of an abstract.

Excerpt

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...

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