RRC ID 3296
著者 Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E.
タイトル Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.
ジャーナル Proc Natl Acad Sci U S A
Abstract We report that human acetyl-CoA synthetase 2 (AceCS2) is a mitochondrial matrix protein. AceCS2 is reversibly acetylated at Lys-642 in the active site of the enzyme. The mitochondrial sirtuin SIRT3 interacts with AceCS2 and deacetylates Lys-642 both in vitro and in vivo. Deacetylation of AceCS2 by SIRT3 activates the acetyl-CoA synthetase activity of AceCS2. This report identifies the first acetylated substrate protein of SIRT3. Our findings show that a mammalian sirtuin directly controls the activity of a metabolic enzyme by means of reversible lysine acetylation. Because the activity of a bacterial ortholog of AceCS2, called ACS, is controlled via deacetylation by a bacterial sirtuin protein, our observation highlights the conservation of a metabolic regulatory pathway from bacteria to humans.
巻・号 103(27)
ページ 10224-10229
公開日 2006-7-5
DOI 10.1073/pnas.0603968103
PII 0603968103
PMID 16788062
PMC PMC1502439
MeSH Acetate-CoA Ligase / chemistry Acetate-CoA Ligase / genetics Acetate-CoA Ligase / metabolism* Acetylation Amino Acid Sequence Animals Binding Sites Cell Line Chlorocebus aethiops Conserved Sequence Humans Lysine / genetics Lysine / metabolism* Mitochondria / enzymology* Mitochondrial Proteins / genetics Mitochondrial Proteins / metabolism Molecular Sequence Data Sequence Alignment Sirtuin 3 Sirtuins / genetics Sirtuins / metabolism
IF 9.412
引用数 499
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
原核生物(大腸菌) JW1106