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

Gregory R. Wagner, R. Payne

Research output: Contribution to journalArticle

225 Citations (Scopus)

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

Fingerprint

Acetylation
Acylation
Acyl Coenzyme A
Mitochondria
Enzymes
Proteins
Lysine

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix. / Wagner, Gregory R.; Payne, R.

In: Journal of Biological Chemistry, Vol. 288, No. 40, 04.10.2013, p. 29036-29045.

Research output: Contribution to journalArticle

@article{62d10a9bf05947d6ad428ece472d775e,
title = "Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix",
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.",
author = "Wagner, {Gregory R.} and R. Payne",
year = "2013",
month = "10",
day = "4",
doi = "10.1074/jbc.M113.486753",
language = "English",
volume = "288",
pages = "29036--29045",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "40",

}

TY - JOUR

T1 - Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix

AU - Wagner, Gregory R.

AU - Payne, R.

PY - 2013/10/4

Y1 - 2013/10/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84885155285&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84885155285&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.486753

DO - 10.1074/jbc.M113.486753

M3 - Article

C2 - 23946487

AN - SCOPUS:84885155285

VL - 288

SP - 29036

EP - 29045

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 40

ER -