Sir2 and the Acetyltransferase, Pat, Regulate the Archaeal Chromatin Protein, Alba

The DNA binding affinity of Alba, a chromatin protein of the archaeon Sulfolobus solfataricus P2, is regulated by acetylation of lysine 16. Here we identify an acetyltransferase that specifically acetylates Alba on this residue. The effect of acetylation is to lower the affinity of Alba for DNA. Rem...

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Veröffentlicht in:	The Journal of biological chemistry 2005-06, Vol.280 (22), p.21122-21128
Hauptverfasser:	Marsh, Victoria L., Peak-Chew, Sew Yeu, Bell, Stephen D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetyltransferases - chemistry Acetyltransferases - metabolism Acetyltransferases - physiology Amino Acid Motifs Amino Acid Sequence Archaea Archaeal Proteins - chemistry Archaeal Proteins - metabolism Chromatin - chemistry Chromatin - metabolism Chromatin Immunoprecipitation Cloning, Molecular DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Gene Expression Regulation Gene Expression Regulation, Archaeal Lysine - chemistry Mass Spectrometry Molecular Sequence Data Open Reading Frames Sirtuins - chemistry Sirtuins - metabolism Sulfolobus solfataricus Sulfolobus solfataricus - metabolism Temperature
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