PXD014366

PXD014366 is an original dataset announced via ProteomeXchange.

Title	Quantitative proteomic and PTM omic analysis in mycobacteria
Description	Cholesterol of the host macrophage membrane is vital for mycobacterial infection, replication, and persistence. During chronic infection within host lung tissues, cholesterol facilitates the phagocytosis of mycobacteria into macrophages. Cholesterol degradation leads to increased flux of acetyl-coenzyme A (CoA) and propionyl-CoA, providing energy and building blocks for virulence macromolecules as well as donors for global protein acylation. Potential functions of lysine acylation are gradually revealed in bacterial survival and pathogenesis. However, the mycobacterial proteome and posttranslational modification (PTM) changes involved in the cholesterol catabolism bioprocess remain unclear. Here, we used nonpathogenic Mycobacterium smegmatis as a model and simultaneously monitored mycobacterial proteome and acetylome changes in the presence of glucose and cholesterol. We discovered that cholesterol metabolic enzymes were upregulated with respect to both protein expression levels and lysine acylation levels during the metabolic shift from glucose to cholesterol. After that, adenylating enzymes related to cholesterol metabolism were proven to be precisely regulated at the propionylation level by mycobacterial acyltransferase M. smegmatis Kat (MsKat) in response to cellular propionyl-CoA accumulation. Furthermore, the kinase expression and phosphorylation levels were also changed along with fluctuations in cholesterol levels. Our results expanded current knowledge of acylation regulation in the cholesterol catabolism of mycobacteria and provided references for possible antimycobacterium strategy.IMPORTANCE Cholesterol assimilation is a critical step in mycobacterial chronic infection. However, knowledge from the dynamic characterization of cholesterol metabolism in mycobacteria at the protein expression and PTM levels remains limited. Our study uncovered the landscape of protein expression, lysine acetylation, lysine propionylation, and S/T/Y phosphorylation during the metabolic changes from glucose to cholesterol in mycobacteria. The data showed that cholesterol-induced carbon shift resulted in the elevation of protein expression and lysine acylation in diverse metabolic enzymes involved in cholesterol degradation and that the presence of cholesterol also promoted the perturbations at the phosphorylation level in the kinase system in mycobacteria. This study systematically characterized the regulation of cholesterol catabolism at several different levels, which provided the detailed references in mycobacterial proteome and potential antimycobacterial strategies.
HostingRepository	iProX
AnnounceDate	2019-12-03
AnnouncementXML	Submission_2020-09-03_22:17:38.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Junyu Xu
SpeciesList	scientific name: Mycobacterium smegmatis MC2 51; NCBI TaxID: 1445611;
ModificationList	propanoylated residue; acetylated residue; phosphorylated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2019-06-24 23:57:15	ID requested
1	2019-12-03 20:37:33	announced
⏵ 2	2020-09-03 22:17:39	announced	2020-09-04: Update publication information

Xu JY, Zhao L, Xu Y, Li B, Zhai L, Tan M, Ye BC, Dynamic Characterization of Protein and Posttranslational Modification Levels in Mycobacterial Cholesterol Catabolism. mSystems, 5(1):(2020) [pubmed]

submitter keyword: quantitative acetylome, quantitative propionylome, quantitative phosphorylome, quantitative proteome

Minjia Tan
contact affiliation	Chinese Academy of Sciences Shanghai Institute of Materia Medica
contact email	mjtan@simm.ac.cn
lab head
Junyu Xu
contact affiliation	Chinese Academy of Sciences Shanghai Institute of Materia Medica
contact email	XJY89089@163.com
dataset submitter

iProX dataset URI