PXD006630

PXD006630 is an original dataset announced via ProteomeXchange.

Title	Nε- and O-Acetylation in Mycobacterium tuberculosis Lineage 7 is Biased Towards Proteins Involved in Growth, Virulence and Antimicrobial Resistance
Description	Protein acetylation is one of the post-translational modifications (PTMs) involved in regulating a myriad of cellular processes in bacteria. Increasing evidence demonstrates that lysine acetylation is involved in Mycobacterium tuberculosis (Mtb) virulence and pathogenesis. However, previous reports have detected acetylation at lysine residues using only reference strains. Here, we analyzed the global Nε- and O-acetylation of Mtb lineage 7 clinical isolates and H37Rv. Quantitative acetylome analysis resulted in identification of 2577 class-I acetylation sites derived from 987 proteins. These proteins were found to be involved in central metabolism, translation, stress responses and drug resistance. Interestingly, 261 acetylation sites on 164 proteins were differentially regulated between the two virulent strains. A total of 257 acetylation sites on 160 proteins were hypoacetylated in lineage 7. These proteins are involved in Mtb growth, virulence, energy metabolism, host-pathogen interaction and stress responses. Furthermore, Gene Ontology (GO) analysis of exclusively acetylated proteins identified revealed strain-specific enrichment of selected biological processes. Taken together, this study provides the first global analysis of O-acetylated proteins in Mtb. This quantitative acetylome data presents the abundance and diversity of acetylated proteins in Mtb and opens a new avenue of research in exploring the role of protein acetylation in fine-tuning Mtb physiology.
HostingRepository	PRIDE
AnnounceDate	2018-05-02
AnnouncementXML	Submission_2018-05-02_00:22:35.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alemayehu Godana Birhanu
SpeciesList	scientific name: Mycobacterium tuberculosis H37Rv; NCBI TaxID: 83332;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-05-30 23:25:34	ID requested
⏵ 1	2018-05-02 00:22:36	announced

Birhanu AG, Yimer SA, Holm-Hansen C, Norheim G, Aseffa A, Abebe M, T, ø, njum T, - and O-Acetylation in Mycobacterium tuberculosis Lineage 7 and Lineage 4 Strains: Proteins Involved in Bioenergetics, Virulence, and Antimicrobial Resistance Are Acetylated. J Proteome Res, 16(11):4045-4059(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: Mycobacterium tuberculosis

lineage 7

post-translational modifications

acetylome

Nε-acetylation

O-acetylation.

Tone Tonjum
contact affiliation	Department of Microbiology, Institute of clinical medicine, University of Oslo, Norway (Group leader )
contact email	tone.tonjum@medisin.uio.no
lab head
Alemayehu Godana Birhanu
contact affiliation	Department of Microbiology,Institute of clinical medicine, University of Oslo, Norway ( Group leader )
contact email	alexbiology97@yahoo.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006630
     1. Label: PRIDE project
     2. Name: Nε- and O-Acetylation in Mycobacterium tuberculosis Lineage 7 is Biased Towards Proteins Involved in Growth, Virulence and Antimicrobial Resistance