| Literature DB >> 11028911 |
Abstract
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.Entities:
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Year: 2000 PMID: 11028911 DOI: 10.1007/pl00000758
Source DB: PubMed Journal: Cell Mol Life Sci ISSN: 1420-682X Impact factor: 9.261