ArticleProtein science : a publication of the Protein Society2006
Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Activity of Membrane-Permeabilizing Lpt Peptides.Biomolecules · 2024Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Identification and characterization of the bacteriocin Carocin S3 from the multiple bacteriocin producing strain of Pectobacterium carotovorum subsp. carotovorum.BMC microbiology · 2020Article
- The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features.Journal of molecular biology · 2019Article
- Can't you hear me knocking: contact-dependent competition and cooperation in bacteria.Emerging topics in life sciences · 2017Article
- The Stable Interaction Between Signal Peptidase LepB of Escherichia coli and Nuclease Bacteriocins Promotes Toxin Entry into the Cytoplasm.The Journal of biological chemistry · 2015Article
- Contact-dependent growth inhibition toxins exploit multiple independent cell-entry pathways.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria.Molecular microbiology · 2014Article
- In vivo processing of DNase colicins E2 and E7 is required for their import into the cytoplasm of target cells.PloS one · 2014Article
- Interaction of nuclease colicins with membranes: insertion depth correlates with bilayer perturbation.PloS one · 2012Article
- FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm.The Journal of biological chemistry · 2011Article
- Cloning, purification, and functional characterization of Carocin S2, a ribonuclease bacteriocin produced by Pectobacterium carotovorum.BMC microbiology · 2011Article
- Swimming against the tide: progress and challenges in our understanding of colicin translocation.Nature reviews. Microbiology · 2010Review
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Nuclease type colicins and related bacteriocins possess the unprecedented ability to translocate an enzymatic polypeptide chain across the Gram-negative cell envelope. Here we use the rRNase domain of the cytotoxic ribonuclease colicin E3 to examine the structural changes on its interaction with the membrane. Using phospholipid vesicles as model membranes we show that anionic membranes destabilize the nuclease domain of the rRNase type colicin E3. Intrinsic tryptophan fluorescence and circular dichroism show that vesicles consisting of pure DOPA act as a powerful protein denaturant toward the rRNase domain, although this interaction can be entirely prevented by the addition of salt. Binding of E3 rRNase to DOPA vesicles is an endothermic process (DeltaH=24 kcal mol-1), reflecting unfolding of the protein. Consistent with this, binding of a highly destabilized mutant of the E3 rRNase to DOPA vesicles is exothermic. With mixed vesicles containing anionic and neutral phospholipids at a ratio of 1:3, set to mimic the charge of the Escherichia coli inner membrane, destabilization of E3 rRNase is lessened, although the melting temperature of the protein at pH 7.0 is greatly reduced from 50 degrees C to 30 degrees C. The interaction of E3 rRNase with 1:3 DOPA:DOPC vesicles is also highly dependent on both ionic strength and temperature. We discuss these results in terms of the likely interaction of the E3 rRNase and the related E9 DNase domains with the E. coli inner membrane and their subsequent translocation to the cell cytoplasm.
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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.