Protein acetylation plays a crucial role in regulating transcriptional activity. Acetylation complexes (such as CBP/p300) or deacetylation complexes (such as HDAC) can be recruited to DNA-bound transcription factors (TF) in response to signaling pathways. Histone hyper-acetylation by histone acetyl-transferases (HATs) is associated with transcriptional activation, presumably by remodeling nucleosomal structure into an open conformation more accessible to transcription complexes. Conversely, histone de-acetylation is associated with transcriptional repression reversing the chromatin remodeling process. Several transcriptional co-activators and co-repressors possess intrinsic acetylase or deacetylase enzymatic activities, respectively. Site-specific acetylation of a growing list of non-histone proteins, including p53 and E2F, has been shown to play an important role in transcriptional regulation and cell proliferation.
References
Chen, H. et al. (1999) Regulation of hormone-induced histone hyperacetylation
and gene activation via acetylation of an acetylase. Cell 98, 675–86.
Herrera, J.E. et al. (1999) Specific acetylation of chromosomal protein
HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol.
19, 3466–3473.
Liu, L. et al. (1999). p53 sites acetylated in vitro by PCAF and p300
are acetylated in vivo in response to DNA damage. Mol. Cell Biol. 19, 1202–1209.
Struhl, K. (1998) Histone acetylation and transcriptional regulatory
mechanisms. Genes Dev. 12, 599–606.
Copyright © 2001-2005 Daniele Focosi.
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