Global histone acetylation and deacetylation in yeast
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/35044127.pdf
Reference29 articles.
1. Georgakopoulos, T. & Thireos, G. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11, 4145–4152 (1992).
2. Brownell, J. E. et al. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843–851 ( 1996).
3. Drysdale, C. M. et al. The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gcn5p coactivator complex. Mol. Cell. Biol. 18, 1711– 1724 (1998).
4. Kadosh, D. & Struhl, K. Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo. Mol. Cell. Biol. 18, 5121–5127 (1998).
5. Rundlett, S. E., Carmen, A. A., Suka, N., Turner, B. M. & Grunstein, M. Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature 392, 831–835 (1998).
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