Structure and Mechanism of Action of the Histone Acetyltransferase Gcn5 and Similarity to Other N-Acetyltransferases

In this issue of the "Proceedings," Trievel et al report the crystal structure of the catalytic HAT domain of yeast GCN5. This domain encompasses residues 99-262 of the 439-aa protein.

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Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1999-08, Vol.96 (16), p.8807-8808
Hauptverfasser:	Sternglanz, Rolf, Schindelin, Hermann
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Acetyltransferases - chemistry Acetyltransferases - metabolism Animals Catalysis Commentary Conserved Sequence Crystallography DNA-Binding Proteins Enzyme substrates Enzymes Fungal Proteins - chemistry Fungal Proteins - metabolism Genes Histone Acetyltransferases Histones Nucleosomes Protein Conformation Protein Kinases - chemistry Protein Kinases - metabolism Protein Structure, Secondary Proteins Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Yeast Yeasts
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Beschreibung
Zusammenfassung:	In this issue of the "Proceedings," Trievel et al report the crystal structure of the catalytic HAT domain of yeast GCN5. This domain encompasses residues 99-262 of the 439-aa protein.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.96.16.8807