Regulation of gene expression by transcription factor acetylation (original) (raw)

Cell Mol Life Sci. 2000 Aug; 57(8-9): 1184–1192.

A. J. Bannister*

Wellcome/CRC Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR (United Kingdom), Fax +44 1223 334089, e-mail: ab149@mole.bio.cam.ac.uk, , , , GB

E. A. Miska

Wellcome/CRC Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR (United Kingdom), Fax +44 1223 334089, e-mail: ab149@mole.bio.cam.ac.uk, , , , GB

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.

Keywords: Key words. Acetyltransferase; histones; acetylation; transcription factors; gene expression; chromatin.

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