Acetylation of Yeast Histone H4 Lysine 16: A Switch for Protein Interactions in Heterochromatin and Euchromatin
This extract was created in the absence of an abstract.
Excerpt
Histone acetylation is an evolutionarily conserved phenomenon that can alter chromatin structure and activity.The basic unit of chromatin, the nucleosome, containstwo molecules of each of the core histones, H3, H4, H2A,and H2B, wrapped by DNA. Each core histone has a central hydrophobic domain that contributes to the histone–histone and histone–DNA contacts that form the basis of the structural organization of the nucleosome(Luger et al. 1997). Extending from the nucleosomalcore, the charged amino- and carboxy-terminal tail domains of the histones are free to interact with linker DNA,adjacent nucleosomes, and other chromosomal proteins(Zheng and Hayes 2003). These tail domains can be modified by acetyltransferases, methyltransferases, and kinases, thus altering their chemical characteristics and,consequently, those of the chromatin fiber...
