Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals 
interact with pyruvate carboxylase and other acetylated biotin-dependent 
carboxylases.

Wirth, M.; Karaca, S.; Wenzel, D.; Ho, L.; Tishkoff, D.; Lombard, D. B.; Verdin, E.; Urlaub, H.; Jedrusik-Bode, M.; Fischle, W.

doi:10.1016/j.mito.2013.02.002

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Journal Article

Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases.

MPS-Authors

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Wirth, M.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons85360

Karaca, S.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16007

Wenzel, D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub, H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14868

Jedrusik-Bode, M.
Department of Genes and Behavior, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15074

Fischle, W.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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http://www.sciencedirect.com/science?_ob=MiamiImageURL&_cid=272218&_user=38661&_pii=S1567724913000263&_check=y&_origin=article&_zone=toolbar&_coverDate=21-Feb-2013&view=c&originContentFamily=serial&wchp=dGLzVlt-zSkWz&md5=40a1446efa5cafb1a48bcb0e44e69f49&pid=1-s2.0-S1567724913000263-main.pdf
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Supplementary Material (public)

1744051-Suppl-1.pdf
(Supplementary material), 130KB

1744051-Suppl-2.pdf
(Supplementary material), 209KB

1744051-Suppl-3.pdf
(Supplementary material), 146KB

1744051-Suppl-4.pdf
(Supplementary material), 891KB

1744051-Suppl-5.pdf
(Supplementary material), 25KB

1744051-Suppl-6.pdf
(Supplementary material), 52KB

1744051-Suppl-7.pdf
(Supplementary material), 52KB

Citation

Wirth, M., Karaca, S., Wenzel, D., Ho, L., Tishkoff, D., Lombard, D. B., et al. (2013). Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases. Mitochondrion, 13(6), 705-720. doi:10.1016/j.mito.2013.02.002.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000E-FC29-F

Abstract

The biological and enzymatic function of SIRT4 is largely uncharacterized. We show that the Caenorhabditis elegans SIR-2.2 and SIR-2.3 orthologs of SIRT4 are ubiquitously expressed, also localize to mitochondria and function during oxidative stress. Further, we identified conserved interaction with mitochondrial biotin-dependent carboxylases (PC, PCC, MCCC), key enzymes in anaplerosis and ketone body formation. The carboxylases were found acetylated on multiple lysine residues and detailed analysis of mPC suggested that one of these residues, K748ac, might regulate enzymatic activity. Nevertheless, no changes in mPC acetylation levels and enzymatic activity could be detected upon overexpression or loss of functional SIRT4.