Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix

Gregory R. Wagner, R. Mark Payne

Research output: Contribution to journalArticle

236 Scopus citations

Abstract

Background:The mechanisms initiating protein acylation in mitochondria are unknown. Results:The pH and acyl-CoA concentrations of the mitochondrial matrix are sufficient to cause protein lysine acetylation and succinylation. Conclusion:Protein acylation in mitochondria may be a nonenzymatic event facilitated by the alkaline pH and high acyl-CoA concentrations. Significance:The mitochondrial deacylases SIRT3 and SIRT5 may have evolved to regulate nonenzymatic protein acylation.

Original languageEnglish (US)
Pages (from-to)29036-29045
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number40
DOIs
StatePublished - Oct 4 2013

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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