ArticleThe Journal of general physiology2000
Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end?
Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- ABPs: diffusible antibacterial toxins secreted by and active against diverse gram-positive bacteria.Infection and immunity · 2026Review
- Chromogranin B (CHGB) is dimorphic and responsible for dominant anion channels delivered to cell surface via regulated secretion.Frontiers in molecular neuroscience · 2023Article
- Colicin U from Shigella boydii Forms Voltage-Dependent Pores.Journal of bacteriology · 2019Article
- Cooperativity and Steep Voltage Dependence in a Bacterial Channel.International journal of molecular sciences · 2019Article
- Mapping the membrane topography of the TH6-TH7 segment of the diphtheria toxin T-domain channel.The Journal of general physiology · 2015Article
- Alpha-synuclein lipid-dependent membrane binding and translocation through the α-hemolysin channel.Biophysical journal · 2014Article
- Protein arcs may form stable pores in lipid membranes.Biophysical journal · 2014Article
- Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state.Biochemistry · 2013Article
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
- Conformational switching of the diphtheria toxin T domain.Journal of molecular biology · 2010Article
- The colicin Ia receptor, Cir, is also the translocator for colicin Ia.Molecular microbiology · 2010Article
- Oligomeric structure of colicin ia channel in lipid bilayer membranes.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
- Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.The EMBO journal · 2007Article
- Protein translocation by bacterial toxin channels: a comparison of diphtheria toxin and colicin Ia.Biophysical journal · 2006Article
- Gating movements of colicin A and colicin Ia are different.The Journal of membrane biology · 2004Article
- Sizing the protein translocation pathway of colicin Ia channels.The Journal of general physiology · 2003Article
- Tuning the membrane surface potential for efficient toxin import.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Translocation of a functional protein by a voltage-dependent ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Colicin Ia, a 626-residue bactericidal protein, consists of three domains, with the carboxy-terminal domain (C domain) responsible for channel formation. Whole colicin Ia or C domain added to a planar lipid bilayer membrane forms voltage-gated channels. We have shown previously that the channel formed by whole colicin Ia has four membrane-spanning segments and an approximately 68-residue segment translocated across the membrane. Various experimental interventions could cause a longer or shorter segment within the C domain to be translocated, making us wonder why translocation normally stops where it does, near the amino-terminal end of the C domain (approximately residue 450). We hypothesized that regions upstream from the C domain prevent its amino-terminal end from moving into and across the membrane. To test this idea, we prepared C domain with a ligand attached near its amino terminus, added it to one side of a planar bilayer to form channels, and then probed from the opposite side with a water-soluble protein that can specifically bind the ligand. The binding of the probe had a dramatic effect on channel gating, demonstrating that the ligand (and hence the amino-terminal end of the C domain) had moved across the membrane. Experiments with larger colicin Ia fragments showed that a region of more than 165 residues, upstream from the C domain, can also move across the membrane. All of the colicin Ia carboxy-terminal fragments that we examined form channels that pass from a state of relatively normal conductance to a low-conductance state; we interpret this passage as a transition from a channel with four membrane-spanning segments to one with only three.
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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.