The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and Its Regulation by Acetylation
| Autor: | Malcolm F. White, Stephen P. Jackson, Catherine H. Botting, Benjamin N. Wardleworth, Stephen D. Bell |
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| Rok vydání: | 2016 |
| Předmět: |
Transcription
Genetic Archaeal Proteins Recombinant Fusion Proteins Saccharomyces cerevisiae Molecular Sequence Data Plasma protein binding Histone Deacetylases Sulfolobus Sirtuin 2 Transcription (biology) Sirtuins Amino Acid Sequence Silent Information Regulator Proteins Saccharomyces cerevisiae Multidisciplinary biology Protein deacetylase activity Acetylation DNA Templates Genetic biology.organism_classification Chromatin Molecular Weight enzymes and coenzymes (carbohydrates) Histone Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Trans-Activators NAD+ kinase Gene Expression Regulation Archaeal Protein Binding |
| Popis: | The conserved Sir2 family of proteins has protein deacetylase activity that is dependent on NAD (the oxidized form of nicotinamide adenine dinucleotide). Although histones are one likely target for the enzymatic activity of eukaryotic Sir2 proteins, little is known about the substrates and roles of prokaryotic Sir2 homologs. We reveal that an archaeal Sir2 homolog interacts specifically with the major archaeal chromatin protein, Alba, and that Alba exists in acetylated and nonacetylated forms. Furthermore, we show that Sir2 can deacetylate Alba and mediate transcriptional repression in a reconstituted in vitro transcription system. These data provide a paradigm for how Sir2 family proteins influence transcription and suggest that modulation of chromatin structure by acetylation arose before the divergence of the archaeal and eukaryotic lineages. |
| Databáze: | OpenAIRE |
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