Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide-Reference-Cited by-同舟云学术

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Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

Published:1999-09 Issue:6748 Volume:401 Page:93-98
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Rojas Jeannie R.,Trievel Raymond C.,Zhou Jianxin,Mo Yi,Li Xinmin,Berger Shelley L.,Allis C. David,Marmorstein Ronen

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/43487.pdf

Reference29 articles.

1. Grant,P. A., Sterner,D. E., Duggan,L. J., Workman,J. L. & Berger,S. L. The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes. Trends Cell Biol. 8, 193–197 (1998).

2. Mizzen,C. A. & Allis,C. D. Linking histone acetylation to transcriptional regulation. Cell. Mol. Life Sci. 54, 6–20 (1998).

3. Trievel,R. C. et al. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl Acad. Sci. USA 96, 8931–8936 (1999).

4. Clements,A. et al. Crystal structure of the histone acetyltransferase domain of the human P/CAF transcriptional regulator bound to coenzyme-A. EMBO J. 18, 3521–3532 (1999).

5. Neuwald,A. F. & Landsman,D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that include the yeast SPT10 protein. Trends Biochem. Sci. 22, 154–155 (1997).

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