ArticleThe Journal of biological chemistry2009
Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Unraveling the Uncharacterized Domain of Carocin S2: A RibonucleaseMicroorganisms · 2022Article
- Toxin import through the antibiotic efflux channel TolC.Nature communications · 2021Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- Decoupling Filamentous Phage Uptake and Energy of the TolQRA Motor in Escherichia coli.Journal of bacteriology · 2020Article
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Directional Porin Binding of Intrinsically Disordered Protein Sequences Promotes Colicin Epitope Display in the Bacterial Periplasm.Biochemistry · 2018Article
- Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli.Nature communications · 2018Article
- Exploitation of an iron transporter for bacterial protein antibiotic import.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Diversity and distribution of nuclease bacteriocins in bacterial genomes revealed using Hidden Markov Models.PLoS computational biology · 2017Article
- Structural and biophysical analysis of nuclease protein antibiotics.The Biochemical journal · 2016Article
- The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria.Molecular microbiology · 2014Article
- Nutrient-responsive regulation determines biodiversity in a colicin-mediated bacterial community.BMC biology · 2014Article
- Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.MicrobiologyOpen · 2013Article
- Overexpression of the Escherichia coli TolQ protein leads to a null-FtsN-like division phenotype.MicrobiologyOpen · 2013Article
- Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.Science (New York, N.Y.) · 2013Article
- A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.PLoS biology · 2013Article
- Interaction of nuclease colicins with membranes: insertion depth correlates with bilayer perturbation.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Nuclease colicins bind their target receptor in the outer membrane of sensitive cells in the form of a high affinity complex with their cognate immunity proteins. Upon cell entry the immunity protein is lost from the complex by means that are poorly understood. We have developed a sensitive fluorescence assay that has enabled us to study the molecular requirements for immunity protein release. Nuclease colicins use members of the tol operon for their translocation across the outer membrane. We have demonstrated that the amino-terminal 80 residues of the colicin E9 molecule, which is the region that interacts with TolB, are essential for immunity protein release. Using tol deletion strains we analyzed the cellular components necessary for immunity protein release and found that in addition to a requirement for tolB, the tolA deletion strain was most affected. Complementation studies showed that the mutation H22A, within the transmembrane segment of TolA, abolishes immunity protein release. Investigation of the energy requirements demonstrated that the proton motive force of the cytoplasmic membrane is critical. Taken together these results demonstrate for the first time a clear energy requirement for the uptake of a nuclease colicin complex and suggest that energy transduced from the cytoplasmic membrane to the outer membrane by TolA could be the driving force for immunity protein release and concomitant translocation of the nuclease domain.
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What OpenQuestion holds
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.