In the nucleus, DNA is tightly packaged into higher-order structures, generating an environment that is highly repressive towards DNA processes such as gene transcription. Acetylation of lysine residues within proteins has recently emerged as a major mechanism used by the cell to overcome this repression. Acetylation of non-histone proteins, including transcription factors, as well as histones, appears to be involved in this process. Like phosphorylation, acetylation is a dynamic process that can regulate protein-DNA and protein-protein interactions. Moreover, a conserved domain, the bromodomain, has been implicated in the binding of acetylated peptides, suggesting a role for acetylation in intracellular signalling.
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Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South KoreaYonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea
Park, Joo-Man
Jo, Seong-Ho
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Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South KoreaYonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea
Jo, Seong-Ho
Kim, Mi-Young
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Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South KoreaYonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea
Kim, Mi-Young
Kim, Tae-Hyun
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Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South KoreaYonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea
Kim, Tae-Hyun
Ahn, Yong-Ho
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Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea
Yonsei Univ, Coll Med, Brain Korea PLUS Project Med Sci 21, Seoul 120752, South KoreaYonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea