ArticleFrontiers in microbiology2015
Comparative Ser/Thr/Tyr phosphoproteomics between two mycobacterial species: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Establishment of a biosafe murine model of skeletal tuberculosis using Mycobacterium smegmatis.Animal models and experimental medicine · 2026Article
- Phosphomimetic mutations near active sites of proteins in Thermus thermophilus suggest a widespread regulatory mechanism.FEBS open bio · 2025Article
- Overexpression of outer membrane protein A (OmpA) increases aminoglycoside sensitivity in mycobacteria.BMC microbiology · 2024Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Identification of Arginine Phosphorylation in Mycolicibacterium smegmatis.Microbiology spectrum · 2022Article
- The Role of Phosphorylation and Acylation in the Regulation of Drug Resistance inBiomedicines · 2022Review
- Targeting the oncogenic TBX3:nucleolin complex to treat multiple sarcoma subtypes.American journal of cancer research · 2021Article
- dbPSP 2.0, an updated database of protein phosphorylation sites in prokaryotes.Scientific data · 2020Article
- Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases.Molecular & cellular proteomics : MCP · 2020Review
- Article
- Identification of Novel Physiological Substrates ofMolecular & cellular proteomics : MCP · 2018Article
- The transpeptidase PbpA and noncanonical transglycosylase RodA ofThe Journal of biological chemistry · 2018Article
- Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.The Journal of biological chemistry · 2016Article
- CTL0511 from Chlamydia trachomatis Is a Type 2C Protein Phosphatase with Broad Substrate Specificity.Journal of bacteriology · 2016Article
- Mass Spectrometry Offers Insight into the Role of Ser/Thr/Tyr Phosphorylation in the Mycobacteria.Frontiers in microbiology · 2016Review
- Mass Spectrometry Targeted Assays as a Tool to Improve Our Understanding of Post-translational Modifications in Pathogenic Bacteria.Frontiers in microbiology · 2016Article
- Proteogenomic Analysis of Mycobacterium smegmatis Using High Resolution Mass Spectrometry.Frontiers in microbiology · 2016Article
- Computational Analysis of the Predicted Evolutionary Conservation of Human Phosphorylation Sites.PloS one · 2016Article
- Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in Bacteria.Frontiers in microbiology · 2016Review
- Regulatory potential of post-translational modifications in bacteria.Frontiers in microbiology · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ser/Thr/Tyr protein phosphorylation plays a critical role in regulating mycobacterial growth and development. Understanding the mechanistic link between protein phosphorylation signaling network and mycobacterial growth rate requires a global view of the phosphorylation events taking place at a given time under defined conditions. In the present study we employed a phosphopeptide enrichment and high throughput mass spectrometry-based strategy to investigate and qualitatively compare the phosphoproteome of two mycobacterial model organisms: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG. Cells were harvested during exponential phase and our analysis detected a total of 185 phospho-sites in M. smegmatis, of which 106 were confidently localized [localization probability (LP) = 0.75; PEP = 0.01]. By contrast, in M. bovis BCG the phosphoproteome comprised 442 phospho-sites, of which 289 were confidently localized. The percentage distribution of Ser/Thr/Tyr phosphorylation was 39.47, 57.02, and 3.51% for M. smegmatis and 35, 61.6, and 3.1% for M. bovis BCG. Moreover, our study identified a number of conserved Ser/Thr phosphorylated sites and conserved Tyr phosphorylated sites across different mycobacterial species. Overall a qualitative comparison of the fast and slow growing mycobacteria suggests that the phosphoproteome of M. smegmatis is a simpler version of that of M. bovis BCG. In particular, M. bovis BCG exponential cells exhibited a much more complex and sophisticated protein phosphorylation network regulating important cellular cycle events such as cell wall biosynthesis, elongation, cell division including immediately response to stress. The differences in the two phosphoproteomes are discussed in light of different mycobacterial growth rates.
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