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Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p

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  • Christian T. Madsen

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen
    Present address: Department of ADME, Novo Nordisk A/S, Novo Nordisk park 1, DK-2760 Måløv, Denmark)

  • Kathrine B. Sylvestersen

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen)

  • Clifford Young

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen)

  • Sara C. Larsen

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen)

  • Jon W. Poulsen

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen)

  • Marianne A. Andersen

    (Section of Integrative Physiology, The Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health Sciences, University of Copenhagen)

  • Eva A. Palmqvist

    (Department of Yeast Physiology and Cultivation)

  • Martin Hey-Mogensen

    (Department of Obesity Biology)

  • Per B. Jensen

    (Department of Obesity Biology)

  • Jonas T. Treebak

    (Section of Integrative Physiology, The Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health Sciences, University of Copenhagen)

  • Michael Lisby

    (University of Copenhagen)

  • Michael L. Nielsen

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen)

Abstract

The essential vitamin biotin is a covalent and tenaciously attached prosthetic group in several carboxylases that play important roles in the regulation of energy metabolism. Here we describe increased acetyl-CoA levels and mitochondrial hyperacetylation as downstream metabolic effects of biotin deficiency. Upregulated mitochondrial acetylation sites correlate with the cellular deficiency of the Hst4p deacetylase, and a biotin-starvation-induced accumulation of Hst4p in mitochondria supports a role for Hst4p in lowering mitochondrial acetylation. We show that biotin starvation and knockout of Hst4p cause alterations in cellular respiration and an increase in reactive oxygen species (ROS). These results suggest that Hst4p plays a pivotal role in biotin metabolism and cellular energy homeostasis, and supports that Hst4p is a functional yeast homologue of the sirtuin deacetylase SIRT3. With biotin deficiency being involved in various metabolic disorders, this study provides valuable insight into the metabolic effects biotin exerts on eukaryotic cells.

Suggested Citation

  • Christian T. Madsen & Kathrine B. Sylvestersen & Clifford Young & Sara C. Larsen & Jon W. Poulsen & Marianne A. Andersen & Eva A. Palmqvist & Martin Hey-Mogensen & Per B. Jensen & Jonas T. Treebak & M, 2015. "Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p," Nature Communications, Nature, vol. 6(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8726
    DOI: 10.1038/ncomms8726
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