ArticleThe Journal of membrane biology1997
Transmembrane insertion of the colicin Ia hydrophobic hairpin.
Article in The Journal of membrane biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 93 citations in OpenAlex.
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Cation channel conductance and pH gating of the innate immunity factor APOL1 are governed by pore-lining residues within the C-terminal domain.The Journal of biological chemistry · 2020Article
- A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lipid-Assisted Membrane Protein Folding and Topogenesis.The protein journal · 2019Review
- Crystal structure of theThe Journal of biological chemistry · 2018Article
- Apolipoprotein L1 confers pH-switchable ion permeability to phospholipid vesicles.The Journal of biological chemistry · 2017Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.The Journal of membrane biology · 2015Review
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
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- Article
- Oligomeric structure of colicin ia channel in lipid bilayer membranes.The Journal of biological chemistry · 2009Article
- Development of a novel small antibody that retains specificity for tumor targeting.Journal of experimental & clinical cancer research : CR · 2009Article
- Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain.The Journal of biological chemistry · 2009Article
- Identification of channel-lining amino acid residues in the hydrophobic segment of colicin Ia.The Journal of general physiology · 2008Article
- Effect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes.Journal of molecular biology · 2007Article
- Using model membrane-inserted hydrophobic helices to study the equilibrium between transmembrane and nontransmembrane states.The Journal of general physiology · 2007Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- An amino acid "transmembrane tendency" scale that approaches the theoretical limit to accuracy for prediction of transmembrane helices: relationship to biological hydrophobicity.Protein science : a publication of the Protein Society · 2006Article
- A novel engineered peptide, a narrow-spectrum antibiotic, is effective against vancomycin-resistant Enterococcus faecalis.Antimicrobial agents and chemotherapy · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Colicin Ia is a bactericidal protein that forms voltage-dependent, ion-conducting channels, both in the inner membrane of target bacteria and in planar bilayer membranes. Its amino acid sequence is rich in charged residues, except for a hydrophobic segment of 40 residues near the carboxyl terminus. In the crystal structure of colicin Ia and related colicins, this segment forms an alpha-helical hairpin. The hydrophobic segment is thought to be involved in the initial association of the colicin with the membrane and in the formation of the channel, but various orientations of the hairpin with respect to the membrane have been proposed. To address this issue, we attached biotin to a residue at the tip of the hydrophobic hairpin, and then probed its location with the biotin-binding protein streptavidin, added to one side or the other of a planar bilayer. Streptavidin added to the same side as the colicin prevented channel opening. Prior addition of streptavidin to the opposite side protected channels from this effect, and also increased the rate of channel opening; it produced these effects even before the first opening of the channels. These results suggest a model of membrane association in which the colicin first binds with the hydrophobic hairpin parallel to the membrane; next the hairpin inserts in a transmembrane orientation; and finally the channel opens. We also used streptavidin binding to obtain a stable population of colicin molecules in the membrane, suitable for the quantitative study of voltage-dependent gating. The effective gating charge thus determined is pH-independent and relatively small, compared with previous results for wild-type colicin Ia.
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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.