ArticleJournal of bacteriology2008
Identification of functional Tat signal sequences in Mycobacterium tuberculosis proteins.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 89 citations in OpenAlex.
- The peptidoglycan-binding domain regulates antimycobacterial activity of LysB by affecting its transportation and/or catalytic activity.Communications biology · 2026Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Metabolic Tagging Reveals Surface-Associated Lipoproteins in Mycobacteria.ACS infectious diseases · 2025Article
- Metabolic tagging reveals surface-associated lipoproteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- The roles of highly conserved, non-catalytic residues in class A β-lactamases.Protein science : a publication of the Protein Society · 2022Article
- A d-Phenylalanine-Benzoxazole Derivative Reveals the Role of the Essential Enzyme Rv3603c in the Pantothenate Biosynthetic Pathway ofACS infectious diseases · 2022Article
- Comparison of carbohydrate ABC importers from Mycobacterium tuberculosis.BMC genomics · 2021Article
- The G132S Mutation Enhances the Resistance ofBiochemistry · 2021Article
- Article
- Engineering a new vaccine platform for heterologous antigen delivery in live-attenuatedComputational and structural biotechnology journal · 2021Article
- ATP-binding cassette (ABC) import systems ofEmerging microbes & infections · 2020Review
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Screening Mycobacterium tuberculosis Secreted Proteins Identifies Mpt64 as a Eukaryotic Membrane-Binding Bacterial Effector.mSphere · 2019Article
- Arginine-deprivation-induced oxidative damage sterilizesProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Genome wide identification and experimental validation of Pseudomonas aeruginosa Tat substrates.Scientific reports · 2018Article
- Compartment-Specific Labeling of Bacterial Periplasmic Proteins by Peroxidase-Mediated Biotinylation.ACS infectious diseases · 2018Article
- Imaging mycobacterial growth and division with a fluorogenic probe.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Phosphate Promotes the Recovery of Mycobacterium tuberculosis β-Lactamase from Clavulanic Acid Inhibition.Biochemistry · 2017Article
- The EXIT Strategy: an Approach for Identifying Bacterial Proteins Exported during Host Infection.mBio · 2017Article
- TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex.The Biochemical journal · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The twin-arginine translocation (Tat) pathway is a system used by some bacteria to export proteins out from the cytosol to the cell surface or extracellular environment. A functional Tat pathway exists in the important human pathogen Mycobacterium tuberculosis. Identification of the substrates exported by the Tat pathway can help define the role that this pathway plays in the physiology and pathogenesis of M. tuberculosis. Here we used a reporter of Tat export, a truncated beta-lactamase, 'BlaC, to experimentally identify M. tuberculosis proteins with functional Tat signal sequences. Of the 13 proteins identified, one lacks the hallmark of a Tat-exported substrate, the twin-arginine dipeptide, and another is not predicted by in silico analysis of the annotated M. tuberculosis genome. Full-length versions of a subset of these proteins were tested to determine if the native proteins are Tat exported. For three proteins, expression in a Deltatat mutant of Mycobacterium smegmatis revealed a defect in precursor processing compared to expression in the wild type, indicating Tat export of the full-length proteins. Conversely, two proteins showed no obvious Tat export in M. smegmatis. One of this latter group of proteins was the M. tuberculosis virulence factor phospholipase C (PlcB). Importantly, when tested in M. tuberculosis a different result was obtained and PlcB was exported in a twin-arginine-dependent manner. This suggests the existence of an M. tuberculosis-specific factor(s) for Tat export of a proven virulence protein. It also emphasizes the importance of domains beyond the Tat signal sequence and bacterium-specific factors in determining if a given protein is Tat exported.
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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.