Steps toward understanding the inheritance of repressive methyl-lysine marks in histones
D Reinberg1, S Chuikov, P Farnham
1Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Cold Spring Harbor Symposia on Quantitative Biology
|August 25, 2005
Abstract
No abstract available in 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.
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