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The Arabidopsis class II sirtuin is a lysine deacetylase and interacts with mitochondrial energy metabolism.
König, Ann-Christine; Hartl, Markus; Pham, Phuong Anh; Laxa, Miriam; Boersema, Paul J; Orwat, Anne; Kalitventseva, Ievgeniia; Plöchinger, Magdalena; Braun, Hans-Peter; Leister, Dario; Mann, Matthias; Wachter, Andreas; Fernie, Alisdair R; Finkemeier, Iris.
Afiliação
  • König AC; Department I of Biology, Ludwig Maximilians University Munich, Grosshaderner Strasse 2, 82152 Martinsried, Germany.
Plant Physiol ; 164(3): 1401-14, 2014 Mar.
Article em En | MEDLINE | ID: mdl-24424322
The posttranslational regulation of proteins by lysine (Lys) acetylation has recently emerged to occur not only on histones, but also on organellar proteins in plants and animals. In particular, the catalytic activities of metabolic enzymes have been shown to be regulated by Lys acetylation. The Arabidopsis (Arabidopsis thaliana) genome encodes two predicted sirtuin-type Lys deacetylases, of which only Silent Information Regulator2 homolog (SRT2) contains a predicted presequence for mitochondrial targeting. Here, we have investigated the function of SRT2 in Arabidopsis. We demonstrate that SRT2 functions as a Lys deacetylase in vitro and in vivo. We show that SRT2 resides predominantly at the inner mitochondrial membrane and interacts with a small number of protein complexes mainly involved in energy metabolism and metabolite transport. Several of these protein complexes, such as the ATP synthase and the ATP/ADP carriers, show an increase in Lys acetylation in srt2 loss-of-function mutants. The srt2 plants display no growth phenotype but rather a metabolic phenotype with altered levels in sugars, amino acids, and ADP contents. Furthermore, coupling of respiration to ATP synthesis is decreased in these lines, while the ADP uptake into mitochondria is significantly increased. Our results indicate that SRT2 is important in fine-tuning mitochondrial energy metabolism.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Arabidopsis / Proteínas de Arabidopsis / Sirtuínas / Metabolismo Energético / Histona Desacetilases / Lisina / Mitocôndrias Idioma: En Revista: Plant Physiol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Alemanha País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Arabidopsis / Proteínas de Arabidopsis / Sirtuínas / Metabolismo Energético / Histona Desacetilases / Lisina / Mitocôndrias Idioma: En Revista: Plant Physiol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Alemanha País de publicação: Estados Unidos