ArticleFrontiers in microbiology2015
Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 75 citations in OpenAlex.
- Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Review
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Phosphomimetic mutations near active sites of proteins in Thermus thermophilus suggest a widespread regulatory mechanism.FEBS open bio · 2025Article
- Article
- Spatial segregation and aging of metabolic processes underlie phenotypic heterogeneity in mycobacteria.bioRxiv : the preprint server for biology · 2023Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- The protein kinase PknB negatively regulates biosynthesis and trafficking of mycolic acids in mycobacteria.Journal of lipid research · 2020Article
- Potential Plasticity of the Mannoprotein Repertoire Associated toMolecules (Basel, Switzerland) · 2020Article
- Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases.Molecular & cellular proteomics : MCP · 2020Review
- Novel mechanistic insights into physiological signaling pathways mediated by mycobacterial Ser/Thr protein kinases.Genes and immunity · 2019Review
- LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation.Nature communications · 2019Article
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- Identification of Novel Physiological Substrates ofMolecular & cellular proteomics : MCP · 2018Article
- Erwinia amylovora catalases KatA and KatG are virulence factors and delay the starvation-induced viable but non-culturable (VBNC) response.Molecular plant pathology · 2018Article
- Multisystem Analysis ofmBio · 2018Article
- NJournal of proteome research · 2017Article
- Systems proteomics approaches to study bacterial pathogens: application to Mycobacterium tuberculosis.Current opinion in microbiology · 2017Review
- Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.The Journal of biological chemistry · 2016Article
- Ser/Thr Phosphorylation Regulates the Fatty Acyl-AMP Ligase Activity of FadD32, an Essential Enzyme in Mycolic Acid Biosynthesis.The Journal of biological chemistry · 2016Article
- Mass Spectrometry Targeted Assays as a Tool to Improve Our Understanding of Post-translational Modifications in Pathogenic Bacteria.Frontiers in microbiology · 2016Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible protein phosphorylation, regulated by protein kinases and phosphatases, mediates a switch between protein activity and cellular pathways that contribute to a large number of cellular processes. The Mycobacterium tuberculosis genome encodes 11 Serine/Threonine kinases (STPKs) which show close homology to eukaryotic kinases. This study aimed to elucidate the phosphoproteomic landscape of a clinical isolate of M. tuberculosis. We performed a high throughput mass spectrometric analysis of proteins extracted from an early-logarithmic phase culture. Whole cell lysate proteins were processed using the filter-aided sample preparation method, followed by phosphopeptide enrichment of tryptic peptides by strong cation exchange (SCX) and Titanium dioxide (TiO2) chromatography. The MaxQuant quantitative proteomics software package was used for protein identification. Our analysis identified 414 serine/threonine/tyrosine phosphorylated sites, with a distribution of S/T/Y sites; 38% on serine, 59% on threonine and 3% on tyrosine; present on 303 unique peptides mapping to 214 M. tuberculosis proteins. Only 45 of the S/T/Y phosphorylated proteins identified in our study had been previously described in the laboratory strain H37Rv, confirming previous reports. The remaining 169 phosphorylated proteins were newly identified in this clinical M. tuberculosis Beijing strain. We identified 5 novel tyrosine phosphorylated proteins. These findings not only expand upon our current understanding of the protein phosphorylation network in clinical M. tuberculosis but the data set also further extends and complements previous knowledge regarding phosphorylated peptides and phosphorylation sites in M. tuberculosis.
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