ArticleJournal of bacteriology2000
Maturation of IncP pilin precursors resembles the catalytic Dyad-like mechanism of leader peptidases.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 74 citations in OpenAlex.
- Phospholipid-independent biogenesis and function of the RP4 conjugation pilus.Nature communications · 2026Article
- Phospholipid-independent biogenesis of a functional RP4 conjugation pilus.bioRxiv : the preprint server for biology · 2025Article
- Pilin regions that select for the small RNA phages inJournal of virology · 2025Article
- A comprehensive list of genes required for the efficient conjugation of plasmid Rts1 was determined by systematic deletion analysis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024Article
- Inhibition of Plasmid Conjugation inInternational journal of molecular sciences · 2023Article
- Preceding Host History of Conjugative Resistance Plasmids Affects Intra- and Interspecific Transfer Potential from Biofilm.mSphere · 2023Article
- Superior Conjugative Plasmids Delivered by Bacteria to Diverse Fungi.Biodesign research · 2022Article
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- Circular bacteriocins: biosynthesis and mode of action.Applied and environmental microbiology · 2014Review
- Discovering the bacterial circular proteins: bacteriocins, cyanobactins, and pilins.The Journal of biological chemistry · 2012Review
- Processing and maturation of the pilin of the type IV secretion system encoded within the gonococcal genetic island.The Journal of biological chemistry · 2011Article
- Evidence for VirB4-mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system.Journal of bacteriology · 2010Article
- Phylogenomics reveals a diverse Rickettsiales type IV secretion system.Infection and immunity · 2010Review
- Biological diversity of prokaryotic type IV secretion systems.Microbiology and molecular biology reviews : MMBR · 2009Review
- The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009Review
- Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.Natural product reports · 2009Review
- Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates.Journal of the American Chemical Society · 2009Article
- Agrobacterium VirB10 domain requirements for type IV secretion and T pilus biogenesis.Molecular microbiology · 2009Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pilus subunit, the pilin, of conjugative IncP pili is encoded by the trbC gene. IncP pilin is composed of 78 amino acids forming a ring structure (R. Eisenbrandt, M. Kalkum, E.-M. Lai, C. I. Kado, and E. Lanka, J. Biol. Chem. 274:22548-22555, 1999). Three enzymes are involved in maturation of the pilin: LepB of Escherichia coli for signal peptide removal and a yet-unidentified protease for removal of 27 C-terminal residues. Both enzymes are chromosome encoded. Finally, the inner membrane-associated IncP TraF replaces a four-amino-acid C-terminal peptide with the truncated N terminus, yielding the cyclic polypeptide. We refer to the latter process as "prepilin cyclization." We have used site-directed mutagenesis of trbC and traF to unravel the pilin maturation process. Each of the mutants was analyzed for its phenotypes of prepilin cyclization, pilus formation, donor-specific phage adsorption, and conjugative DNA transfer abilities. Effective prepilin cyclization was determined by matrix-assisted laser desorption-ionization-mass spectrometry using an optimized sample preparation technique of whole cells and trans-3-indolyl acrylic acid as a matrix. We found that several amino acid exchanges in the TrbC core sequence allow prepilin cyclization but disable the succeeding pilus assembly. We propose a mechanism explaining how the signal peptidase homologue TraF attacks a C-terminal section of the TrbC core sequence via an activated serine residue. Rather than cleaving and releasing hydrolyzed peptides, TraF presumably reacts as a peptidyl transferase, involving the N terminus of TrbC in the aminolysis of a postulated TraF-acetyl-TrbC intermediate. Under formal loss of a C-terminal tetrapeptide, a new peptide bond is formed in a concerted action, connecting serine 37 with glycine 114 of TrbC.
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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.