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Histone modifications on the adrenergic induction of type II deiodinase in rat pinealocytes

Constance L Chik1, Donald M Price, Anthony K Ho

  • 1Department of Medicine (CLC) and Department of Physiology (DMP, AKH), Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada. cchik@ualberta.ca

Molecular and Cellular Endocrinology
|June 28, 2011
PubMed

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Two...