TY - JOUR
T1 - The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and Its Regulation by Acetylation
AU - Bell, Stephen D
AU - Botting, Catherine Helen
AU - Wardleworth, Benjamin N
AU - Jackson, Stephen P
AU - White, Malcolm Frederick
N1 - Mass spectrometry showed the archaeal chromatin protein, Alba is acetylated. Sir2 interacts specifically with Alba, deacetylating it, thus mediating transcriptional repression in vitro. This paper demonstrated the first acetylation in Archeae implying modulation of chromatin structure by acetylation arose before the divergence of the archaeal and eukaryotic lineages.
PY - 2002/4/5
Y1 - 2002/4/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037023326&partnerID=8YFLogxK
UR - http://dx.doi.org/10.1126/science.1070506
U2 - 10.1126/science.1070506
DO - 10.1126/science.1070506
M3 - Article
SN - 0036-8075
VL - 296
SP - 148
EP - 151
JO - Science
JF - Science
IS - 5565
ER -