ArticleThe Journal of biological chemistry2009
Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher.
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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Reaching the End of the Line: Urinary Tract Infections.Microbiology spectrum · 2019Review
- Therapeutic Approaches Targeting the Assembly and Function of Chaperone-Usher Pili.EcoSal Plus · 2019Review
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Outer membrane protein design.Current opinion in structural biology · 2017Review
- Effect of chaperone-adhesin complex on plug release by the PapC usher.FEBS letters · 2016Article
- Nitazoxanide Inhibits Pilus Biogenesis by Interfering with Folding of the Usher Protein in the Outer Membrane.Antimicrobial agents and chemotherapy · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- The pilus usher controls protein interactions via domain masking and is functional as an oligomer.Nature structural & molecular biology · 2015Article
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Article
- Molecular basis of usher pore gating in Escherichia coli pilus biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ordered and ushered; the assembly and translocation of the adhesive type I and p pili.Biology · 2013Article
- Current fluctuation analysis of the PopB and PopD translocon components of the Pseudomonas aeruginosa type III secretion system.Biophysical journal · 2013Article
- Cation selectivity is a conserved feature in the OccD subfamily of Pseudomonas aeruginosa.Biochimica et biophysica acta · 2012Article
- Article
- The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS.Molecular & cellular proteomics : MCP · 2012Article
- Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Analysis of gating transitions among the three major open states of the OpdK channel.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The chaperone/usher system is one of the best characterized pathways for protein secretion and assembly of cell surface appendages in Gram-negative bacteria. In particular, this pathway is used for biogenesis of the P pilus, a key virulence factor used by uropathogenic Escherichia coli to adhere to the host urinary tract. The P pilus individual subunits bound to the periplasmic chaperone PapD are delivered to the outer membrane PapC usher, which serves as an assembly platform for subunit incorporation into the pilus and secretion of the pilus fiber to the cell surface. PapC forms a dimeric, twin pore complex, with each monomer composed of a 24-stranded transmembrane beta-barrel channel, an internal plug domain that occludes the channel, and globular N- and C-terminal domains that are located in the periplasm. Here we have used planar lipid bilayer electrophysiology to characterize the pore properties of wild type PapC and domain deletion mutants for the first time. The wild type pore is closed most of the time but displays frequent short-lived transitions to various open states. In comparison, PapC mutants containing deletions of the plug domain, an alpha-helix that caps the plug domain, or the N- and C-terminal domains form channels with higher open probability but still exhibiting dynamic behavior. Removal of the plug domain results in a channel with extremely large conductance. These observations suggest that the plug gates the usher channel closed and that the periplasmic domains and alpha-helix function to modulate the gating activity of the PapC twin pore.
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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.