ArticleJournal of bacteriology2007
Porins are required for uptake of phosphates by Mycobacterium smegmatis.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- The accessory role of the outer membrane porin protein MspD inMicrobiology (Reading, England) · 2026Article
- The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 2024Article
- Control of subunit stoichiometry in single-chain MspA nanopores.Biophysical journal · 2022Article
- Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope.Chemical reviews · 2021Review
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Article
- Lipoproteins in Gram-Positive Bacteria: Abundance, Function, Fitness.Frontiers in microbiology · 2020Review
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Article
- The Mycobacterium tuberculosis relBE toxin:antitoxin genes are stress-responsive modules that regulate growth through translation inhibition.Journal of microbiology (Seoul, Korea) · 2015Article
- Surface hydrolysis of sphingomyelin by the outer membrane protein Rv0888 supports replication of Mycobacterium tuberculosis in macrophages.Molecular microbiology · 2015Article
- Essential Role of the ESX-5 Secretion System in Outer Membrane Permeability of Pathogenic Mycobacteria.PLoS genetics · 2015Article
- Porins increase copper susceptibility of Mycobacterium tuberculosis.Journal of bacteriology · 2013Article
- Rhodococcus jostii porin A (RjpA) functions in cholate uptake.Applied and environmental microbiology · 2013Article
- Uptake of sulfate but not phosphate by Mycobacterium tuberculosis is slower than that for Mycobacterium smegmatis.Journal of bacteriology · 2012Article
- Comparative analyses of transport proteins encoded within the genomes of Mycobacterium tuberculosis and Mycobacterium leprae.Biochimica et biophysica acta · 2012Article
- Expression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environments.Molecular microbiology · 2011Article
- Importance of porins for biocide efficacy against Mycobacterium smegmatis.Applied and environmental microbiology · 2011Article
- Ethidium bromide transport across Mycobacterium smegmatis cell-wall: correlation with antibiotic resistance.BMC microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Phosphorus is an essential nutrient, but how phosphates cross the mycobacterial cell wall is unknown. Phosphatase activity in whole cells of Mycobacterium smegmatis was significantly lower than that in lysed cells, indicating that access to the substrate was restricted. The loss of the outer membrane (OM) porin MspA also reduced the phosphatase activity in whole cells compared to that in lysed cells. A similar result was obtained for M. smegmatis that overexpressed endogenous alkaline phosphatase, indicating that PhoA is not a surface protein, contrary to a previous report. The uptake of phosphate by a mutant lacking the porins MspA and MspC was twofold lower than that by wild-type M. smegmatis. Strikingly, the loss of these porins resulted in a severe growth defect of M. smegmatis on low-phosphate plates. We concluded that the OM of M. smegmatis represents a permeability barrier for phosphates and that Msp porins are the only OM channels for the diffusion of phosphate in M. smegmatis. However, phosphate diffusion through Msp pores is rather inefficient as shown by the 10-fold lower permeability of M. smegmatis for phosphate compared to that for glucose. This is likely due to the negative charges in the constriction zone of Msp porins. The phosphatase activity in whole cells of Mycobacterium bovis BCG was significantly less than that in lysed cells, indicating a similar uptake pathway for phosphates in slow-growing mycobacteria. However, porins that could mediate the diffusion of phosphates across the OM of M. bovis BCG and Mycobacterium tuberculosis are unknown.
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Registered trials
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.