ArticleMolecular & cellular proteomics : MCP2015
Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell Wall.
Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 62 citations in OpenAlex.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Secreted proteins ofFrontiers in tuberculosis · 2026Review
- Metabolic Tagging Reveals Surface-Associated Lipoproteins in Mycobacteria.ACS infectious diseases · 2025Article
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Loss of theScience advances · 2025Article
- Development of a brain-penetrant G9a methylase inhibitor to target Alzheimer's disease-associated proteopathology.Nature communications · 2025Article
- Metabolic tagging reveals surface-associated lipoproteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Review
- Proteomics from compartment-specific APEX2 labeling in Mycobacterium tuberculosis reveals Type VII secretion substrates in the cell wall.Cell chemical biology · 2024Article
- Mycobacterium tuberculosis SecA2-dependent activation of host Rig-I/MAVs signaling is not conserved in Mycobacterium marinum.PloS one · 2024Article
- Non-canonical function of histone methyltransferase G9a in the translational regulation of chronic inflammation.Cell chemical biology · 2023Article
- MceG stabilizes the Mce1 and Mce4 transporters in Mycobacterium tuberculosis.The Journal of biological chemistry · 2023Article
- Cyclic AMP is a critical mediator of intrinsic drug resistance and fatty acid metabolism ineLife · 2023Article
- Mycobacterium smegmatis: The Vanguard of Mycobacterial Research.Journal of bacteriology · 2023Review
- Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.Journal of bacteriology · 2021Article
- The genetic proteome: Using genetics to inform the proteome of mycobacterial pathogens.PLoS pathogens · 2021Review
- Article
- Article
- Review
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Mycobacterium tuberculosis is an example of a bacterial pathogen with a specialized SecA2-dependent protein export system that contributes to its virulence. Our understanding of the mechanistic basis of SecA2-dependent export and the role(s) of the SecA2 pathway in M. tuberculosis pathogenesis has been hindered by our limited knowledge of the proteins exported by the pathway. Here, we set out to identify M. tuberculosis proteins that use the SecA2 pathway for their export from the bacterial cytoplasm to the cell wall. Using label-free quantitative proteomics involving spectral counting, we compared the cell wall and cytoplasmic proteomes of wild type M. tuberculosis to that of a ΔsecA2 mutant. This work revealed a role for the M. tuberculosis SecA2 pathway in the cell wall localization of solute binding proteins that work with ABC transporters to import solutes. Another discovery was a profound effect of SecA2 on the cell wall localization of the Mce1 and Mce4 lipid transporters, which contribute to M. tuberculosis virulence. In addition to the effects on solute binding proteins and Mce transporter export, our label-free quantitative analysis revealed an unexpected relationship between SecA2 and the hypoxia-induced DosR regulon, which is associated with M. tuberculosis latency. Nearly half of the transcriptionally controlled DosR regulon of cytoplasmic proteins were detected at higher levels in the ΔsecA2 mutant versus wild type M. tuberculosis. By increasing the list of M. tuberculosis proteins known to be affected by the SecA2 pathway, this study expands our appreciation of the types of proteins exported by this pathway and guides our understanding of the mechanism of SecA2-dependent protein export in mycobacteria. At the same time, the newly identified SecA2-dependent proteins are helpful for understanding the significance of this pathway to M. tuberculosis virulence and physiology.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.