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A systematic evaluation of the compatibility of histones containing methyl-lysine analogues with biochemical

Guangshuai Jia, Weixiang Wang, Hong Li

    Cell Research
    |September 23, 2009
    PubMed
    Abstract

    No abstract available in PubMed .

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    Histone Modification02:32

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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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    The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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