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Science 5 April 2002:
Vol. 296. no. 5565, pp. 148 - 151
DOI: 10.1126/science.1070506
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Reports

The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and Its Regulation by Acetylation

Stephen D. Bell,1* Catherine H. Botting,2 Benjamin N. Wardleworth,2 Stephen P. Jackson,3 Malcolm F. White2*

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.

1 Medical Research Council (MRC) Cancer Cell Unit, The Hutchison/MRC Research Centre, Hills Road, Cambridge, CB2 2QH, UK.
2 Centre for Biomolecular Sciences, St. Andrews University, North Haugh, St. Andrews, Fife, KY16 9ST, UK.
3 Wellcome Trust and Cancer Research Campaign Institute of Cancer and Developmental Biology, Tennis Court Road, Cambridge, CB2 1QR, UK; and Department of Zoology, University of Cambridge, UK.
*   To whom correspondence should be addressed. E-mail: sdb{at}mole.bio.cam.ac.uk and mfw2{at}st-andrews.ac.uk

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