ArticleThe Journal of biological chemistry2011
Charge requirements for proton gradient-driven translocation of anthrax toxin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- A dynamical anthrax toxin nanopore biosensor for high-fidelity single-peptide classification.PLoS computational biology · 2026Article
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- The N-terminus of themBio · 2025Article
- Tetanus ToxinmSphere · 2020Article
- Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.Nature structural & molecular biology · 2020Article
- Structure of a Tc holotoxin pore provides insights into the translocation mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Membrane insertion of a Tc toxin in near-atomic detail.Nature structural & molecular biology · 2016Article
- Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Forces from the Portal Govern the Late-Stage DNA Transport in a Viral DNA Packaging Nanomotor.Biophysical journal · 2016Article
- Tumor Targeting and Drug Delivery by Anthrax Toxin.Toxins · 2016Review
- Peptide Probes Reveal a Hydrophobic Steric Ratchet in the Anthrax Toxin Protective Antigen Translocase.Journal of molecular biology · 2015Article
- Role of the α Clamp in the Protein Translocation Mechanism of Anthrax Toxin.Journal of molecular biology · 2015Article
- Article
- A protective antigen mutation increases the pH threshold of anthrax toxin receptor 2-mediated pore formation.Biochemistry · 2014Article
- Article
- Designing inhibitors of anthrax toxin.Expert opinion on drug discovery · 2014Review
- Anthrax toxin-induced rupture of artificial lipid bilayer membranes.The Journal of chemical physics · 2013Article
- Current fluctuation analysis of the PopB and PopD translocon components of the Pseudomonas aeruginosa type III secretion system.Biophysical journal · 2013Article
- Designed azolopyridinium salts block protective antigen pores in vitro and protect cells from anthrax toxin.PloS one · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
Anthrax lethal toxin is used as a model system to study protein translocation. The toxin is composed of a translocase channel, called protective antigen (PA), and an enzyme, called lethal factor (LF). A proton gradient (ΔpH) can drive LF unfolding and translocation through PA channels; however, the mechanism of ΔpH-mediated force generation, substrate unfolding, and establishment of directionality are poorly understood. One recent hypothesis suggests that the ΔpH may act through changes in the protonation state of residues in the substrate. Here we report the charge requirements of LF's amino-terminal binding domain (LF(N)) using planar lipid bilayer electrophysiology. We found that acidic residues are required in LF(N) to utilize a proton gradient for translocation. Constructs lacking negative charges in the unstructured presequence of LF(N) translocate independently of the ΔpH driving force. Acidic residues markedly increase the rate of ΔpH-driven translocation, and the presequence is optimized in its natural acidic residue content for efficient ΔpH-driven unfolding and translocation. We discuss a ΔpH-driven charge state Brownian ratchet mechanism for translocation, where glutamic and aspartic acid residues in the substrate are the "molecular teeth" of the ratchet. Our Brownian ratchet model includes a mechanism for unfolding and a novel role for positive charges, which we propose chaperone negative charges through the PA channel during ΔpH translocation.
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