Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone

Most histone acetyltransferases (HATs) function as multisubunit complexes in which accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a particularly interesting example of a HAT whose specificity and catalytic activity require association with either of two histone...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2010-11, Vol.107 (47), p.20275-20280
Hauptverfasser:	Kolonko, Erin M., Albaugh, Brittany N., Lindner, Scott E., Chen, Yuanyuan, Satyshur, Kenneth A., Arnold, Kevin M., Kaufman, Paul D., Keck, James L., Denu, John M., Kornberg, Roger D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Biochemical mechanisms Biochemistry Biological Sciences Blotting, Western Catalysis Cell Cycle Proteins - metabolism Chaperones Conformation Crystallization Crystals Dimerization Dimers Electrophoresis, Polyacrylamide Gel Electrostatics Enzyme kinetics Enzymes Genetic analysis Histone acetyltransferase Histone Acetyltransferases - metabolism Histone chaperones Histones Histones - metabolism Kinetics Lysine Mass Spectrometry Models, Molecular Molecular Chaperones - metabolism Molecular modelling Molecular structure Proteins Saccharomyces cerevisiae Proteins - metabolism Side effects Static Electricity Substrate specificity X-Ray Diffraction Yeasts
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