PXD000885

PXD000885 is an original dataset announced via ProteomeXchange.

Title	Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions
Description	Acetylation is frequently detected on mitochondrial enzymes and the sirtuin deacetylase SIRT3 is thought to regulate metabolism by deacetylating mitochondrial proteins. However, the stoichiometry of acetylation has not been studied and is important for understanding whether SIRT3 regulates or suppresses acetylation. Using quantitative mass spectrometry we measured acetylation stoichiometry in mouse liver tissue and found that SIRT3 suppressed acetylation to a very low stoichiometry at its target sites. By examining acetylation changes in the liver, heart, brain, and brown adipose tissue of fasted mice, we found that SIRT3-targeted sites were mostly unaffected by fasting, a dietary manipulation that is thought to regulate metabolism through SIRT3-dependent deacetylation. Globally increased mitochondrial acetylation in fasted liver tissue, higher stoichiometry at mitochondrial acetylation sites, and greater sensitivity of SIRT3-targeted sites to chemical acetylation in vitro and fasting in vivo, suggests a nonenzymatic mechanism of acetylation. Our data indicate that most mitochondrial acetylation occurs as a low-level nonenzymatic protein lesion and that SIRT3 functions as a protein repair factor that removes acetylation lesions from lysine residues.
HostingRepository	PRIDE
AnnounceDate	2015-09-15
AnnouncementXML	Submission_2015-09-15_08:03:52.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Brian Weinert
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	acetylated residue
Instrument	LTQ Orbitrap Velos; Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2014-04-09 02:07:27	ID requested
⏵ 1	2015-09-15 08:03:53	announced

Weinert BT, Moustafa T, Iesmantavicius V, Zechner R, Choudhary C, Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions. EMBO J, 34(21):2620-32(2015) [pubmed]

curator keyword: Biological

submitter keyword: Acetylation, Stoichiometry, Liver, SIRT3

Chuna Choudahary
contact affiliation	NNF Center for Protein Research University of Copenhagen Blegdamsvej 3b, DK-2200 Copenhagen N
contact email	chuna.choudhary@cpr.ku.dk
lab head
Brian Weinert
contact affiliation	Proteomics
contact email	brtw@cpr.ku.dk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD000885
     1. Label: PRIDE project
     2. Name: Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions