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The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autorschaft

  • Ann Christine König
  • Markus Hartl
  • Phuong Anh Pham
  • Miriam Laxa
  • Hans Peter Braun

Organisationseinheiten

Externe Organisationen

  • Ludwig-Maximilians-Universität München (LMU)
  • Max-Planck-Institut für molekulare Pflanzenphysiologie
  • Max-Planck-Institut für Biochemie
  • Eberhard Karls Universität Tübingen

Details

OriginalspracheEnglisch
Seiten (von - bis)1401-1414
Seitenumfang14
FachzeitschriftPlant physiology
Jahrgang164
Ausgabenummer3
PublikationsstatusVeröffentlicht - März 2014

Abstract

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.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Physiologie
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde

Zitieren

The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism. / König, Ann Christine; Hartl, Markus; Pham, Phuong Anh et al.
in: Plant physiology, Jahrgang 164, Nr. 3, 03.2014, S. 1401-1414.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

König, AC, Hartl, M, Pham, PA, Laxa, M, Boersema, PJ, Orwat, A, Kalitventseva, I, Plöchinger, M, Braun, HP, Leister, D, Mann, M, Wachter, A, Fernie, AR & Finkemeier, I 2014, 'The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism', Plant physiology, Jg. 164, Nr. 3, S. 1401-1414. https://doi.org/10.1104/pp.113.232496, https://doi.org/10.15488/11684
König, A. C., Hartl, M., Pham, P. A., Laxa, M., Boersema, P. J., Orwat, A., Kalitventseva, I., Plöchinger, M., Braun, H. P., Leister, D., Mann, M., Wachter, A., Fernie, A. R., & Finkemeier, I. (2014). The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism. Plant physiology, 164(3), 1401-1414. https://doi.org/10.1104/pp.113.232496, https://doi.org/10.15488/11684
König AC, Hartl M, Pham PA, Laxa M, Boersema PJ, Orwat A et al. The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism. Plant physiology. 2014 Mär;164(3):1401-1414. doi: 10.1104/pp.113.232496, 10.15488/11684
König, Ann Christine ; Hartl, Markus ; Pham, Phuong Anh et al. / The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism. in: Plant physiology. 2014 ; Jahrgang 164, Nr. 3. S. 1401-1414.
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title = "The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism",
abstract = "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.",
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T1 - The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism

AU - König, Ann Christine

AU - Hartl, Markus

AU - Pham, Phuong Anh

AU - Laxa, Miriam

AU - Boersema, Paul J.

AU - Orwat, Anne

AU - Kalitventseva, Ievgeniia

AU - Plöchinger, Magdalena

AU - Braun, Hans Peter

AU - Leister, Dario

AU - Mann, Matthias

AU - Wachter, Andreas

AU - Fernie, Alisdair R.

AU - Finkemeier, Iris

PY - 2014/3

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N2 - 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.

AB - 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.

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