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

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, Michael Lisby and Michael L. Nielsen ()
Additional contact information
Christian T. Madsen: The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen
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

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8726

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