ArticleJournal of bacteriology2004
The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 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
40 citing papers in PubMed.
- Biofilm Formation and the Role of Efflux Pumps in ESKAPE Pathogens.Microorganisms · 2025Review
- Structural basis for adhesin secretion by the outer-membrane usher in type 1 pili.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Stochastic chain termination in bacterial pilus assembly.Nature communications · 2023Article
- Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis.Nature communications · 2021Article
- The small molecule nitazoxanide selectively disrupts BAM-mediated folding of the outer membrane usher protein.The Journal of biological chemistry · 2019Article
- The Remarkable Biomechanical Properties of the Type 1 Chaperone-Usher Pilus: A Structural and Molecular Perspective.Microbiology spectrum · 2019Review
- Structural basis for usher activation and intramolecular subunit transfer in P pilus biogenesis in Escherichia coli.Nature microbiology · 2018Article
- Article
- A comprehensive guide to pilus biogenesis in Gram-negative bacteria.Nature reviews. Microbiology · 2017Review
- Nitazoxanide Inhibits Pilus Biogenesis by Interfering with Folding of the Usher Protein in the Outer Membrane.Antimicrobial agents and chemotherapy · 2016Article
- Drug and Vaccine Development for the Treatment and Prevention of Urinary Tract Infections.Microbiology spectrum · 2016Review
- 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
- Article
- Ordered and ushered; the assembly and translocation of the adhesive type I and p pili.Biology · 2013Article
- 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
- Chaperone-usher pathways: diversity and pilus assembly mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli.Journal of bacteriology · 2011Article
- Second order rate constants of donor-strand exchange reveal individual amino acid residues important in determining the subunit specificity of pilus biogenesis.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
Pilus biogenesis on the surface of uropathogenic Escherichia coli requires the chaperone/usher pathway, a terminal branch of the general secretory pathway. In this pathway, periplasmic chaperone-subunit complexes target an outer membrane (OM) usher for subunit assembly into pili and secretion to the cell surface. The molecular mechanisms of protein secretion across the OM are not well understood. Mutagenesis of the P pilus usher PapC and the type 1 pilus usher FimD was undertaken to elucidate the initial stages of pilus biogenesis at the OM. Deletion of residues 2 to 11 of the mature PapC N terminus abolished the targeting of the usher by chaperone-subunit complexes and rendered PapC nonfunctional for pilus biogenesis. Similarly, an intact FimD N terminus was required for chaperone-subunit binding and pilus biogenesis. Analysis of PapC-FimD chimeras and N-terminal fragments of PapC localized the chaperone-subunit targeting domain to the first 124 residues of PapC. Single alanine substitution mutations were made in this domain that blocked pilus biogenesis but did not affect targeting of chaperone-subunit complexes. Thus, the usher N terminus does not function simply as a static binding site for chaperone-subunit complexes but also participates in subsequent pilus assembly events.
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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.