PXD005903

PXD005903 is an original dataset announced via ProteomeXchange.

Title	Integrated lysine acetylation stoichiometry and proteomics analysis in human cells
Description	Lysine acetylation is a widespread posttranslational modification that targets a large number of biological pathways. Recent studies reveal that lysine acetylation sites exhibit mainly low stoichiometry. Here we explored three sample preparation methods, the use of detergents for the chemical acetylation reaction in combination with stable and efficient alkylating reagent, to analyze the stoichiometry of acetylation in three human cell lines. We identified and determined the acetylation occupancy in about 1500 protein in each cell line. Lysine acetylation is highly dynamic, we determined variations in the acetylation stoichiometry when nearby residues are phosphorylated. The stoichiometric analysis in combination with quantitative proteomics allowed us to better understand the role of this PTM in different cells. We found that high abundance of the deacetylase SIRT1 correlates with less acetylation occupancy and abundance of ribosomes, proteins involved in ribosome biogenesis, rRNA processing, among others. We confirmed through the inhibition of SIRT1 with EX-527, followed by quantitative proteomics and acetylation stoichiometry analyzes, the negative role of this deacetylase on transcription and translation pathways. In addition, we found that SIRT1 positively regulates several metabolic pathways.
HostingRepository	PRIDE
AnnounceDate	2017-09-12
AnnouncementXML	Submission_2017-09-18_07:39:32.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jeovanis Gil
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-02-10 03:03:38	ID requested
1	2017-09-12 00:09:13	announced
⏵ 2	2017-09-18 07:39:33	announced	Updated publication reference for PubMed record(s): 28893905.

Gil J, Ram, í, rez-Torres A, Chiappe D, Luna-Pe, ñ, aloza J, Fernandez-Reyes FC, Arcos-Encarnaci, ó, n B, Contreras S, Encarnaci, ó, n-Guevara S, Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells. J Biol Chem, 292(44):18129-18144(2017) [pubmed]

submitter keyword: Lysine Acetylation, SIRT1, Proteomics, Stoichiometry, Cancer cells, Deacetylase inhibitor

Sergio Manuel Encarnación-Guevara
contact affiliation	Programa de Genómica Funcional de Procariontes, Centro de Ciencias Genómicas-UNAM. Av. Universidad s/n, Col. Chamilpa, Cuernavaca, Morelos. CP 62210. México.
contact email	encarnac@ccg.unam.mx
lab head
Jeovanis Gil
contact affiliation	CCG-UNAM
contact email	jeovanis@ccg.unam.mx
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD005903
     1. Label: PRIDE project
     2. Name: Integrated lysine acetylation stoichiometry and proteomics analysis in human cells