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

Wirth, Martina; Karaca, Samir; Wenzel, Dirk; Ho, Linh; Tishkoff, Daniel; Lombard, David B; Verdin, Eric; Urlaub, Henning; Jedrusik-Bode, Monika; Fischle, Wolfgang

Wirth, Martina; Karaca, Samir; Wenzel, Dirk; Ho, Linh; Tishkoff, Daniel; Lombard, David B; Verdin, Eric; Urlaub, Henning; Jedrusik-Bode, Monika; Fischle, Wolfgang.

Affiliation

Wirth M; Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Mitochondrion ; 13(6): 705-20, 2013 Nov.

Article in En | MEDLINE | ID: mdl-23438705

Subject(s)

Biotin/metabolism; Caenorhabditis elegans/metabolism; Mitochondria/metabolism; Mitochondrial Proteins/metabolism; Pyruvate Carboxylase/metabolism; Sirtuins/metabolism; Acetylation; Animals; Animals, Genetically Modified; Chromatography, Liquid; HEK293 Cells; Humans; Mitochondria/enzymology; Oxidative Stress; RNA Interference; Tandem Mass Spectrometry

Key words

Biotin-dependent carboxylase; C. elegans; Protein acetylation; Pyruvate carboxylase; SIRT4; Sirtuins

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pyruvate Carboxylase / Biotin / Caenorhabditis elegans / Mitochondrial Proteins / Sirtuins / Mitochondria Limits: Animals / Humans Language: En Journal: Mitochondrion Year: 2013 Document type: Article Affiliation country: Germany Country of publication: Netherlands

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