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.
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container_title The Journal of biological chemistry
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creator Marsh, Victoria L.
Peak-Chew, Sew Yeu
Bell, Stephen D.
description 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. Remarkably, the acetyltransferase is conserved not only in archaea but also in bacteria where it appears to play a role in metabolic regulation. Therefore, our data suggest that S. solfataricus has co-opted this bacterial regulatory system to generate a rudimentary form of chromatin regulation.
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subjects 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
title Sir2 and the Acetyltransferase, Pat, Regulate the Archaeal Chromatin Protein, Alba
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