ArticleJournal of bacteriology2009
Peptide wrwycr inhibits the excision of several prophages and traps holliday junctions inside bacteria.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Pathological R-loops in bacteria from engineered expression of endogenous antisense RNAs whose synthesis is ordinarily terminated by Rho.Nucleic acids research · 2024Article
- DNA Damage-Inducible Pyocin Expression Is Independent of RecA inMicrobiology spectrum · 2022Article
- Potentiation of Antibiotics by a Novel Antimicrobial Peptide against Shiga Toxin Producing E. coli O157:H7.Scientific reports · 2020Article
- Novel antimicrobial peptide prevents C. rodentium infection in C57BL/6 mice by enhancing acid-induced pathogen killing.Microbiology (Reading, England) · 2016Article
- Hexapeptides that inhibit processing of branched DNA structures induce a dynamic ensemble of Holliday junction conformations.The Journal of biological chemistry · 2015Article
- Targets for Combating the Evolution of Acquired Antibiotic Resistance.Biochemistry · 2015Review
- The λ Integrase Site-specific Recombination Pathway.Microbiology spectrum · 2015Review
- Article
- Antimicrobial metallopeptides with broad nuclease and ribonuclease activity.Chemical communications (Cambridge, England) · 2013Article
- wrwyrggrywrw is a single-chain functional analog of the Holliday junction-binding homodimer, (wrwycr)2.Peptides · 2013Article
- Tumor cell death mediated by peptides that recognize branched intermediates of DNA replication and repair.PloS one · 2013Article
- Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution.Microbiology (Reading, England) · 2012Article
- Similarities between exogenously- and endogenously-induced envelope stress: the effects of a new antibacterial molecule, TPI1609-10.PloS one · 2012Article
- Potent antimicrobial small molecules screened as inhibitors of tyrosine recombinases and Holliday junction-resolving enzymes.Molecular diversity · 2011Article
- Activation of XerCD-dif recombination by the FtsK DNA translocase.Nucleic acids research · 2011Article
- A novel antimicrobial peptide significantly enhances acid-induced killing of Shiga toxin-producing Escherichia coli O157 and non-O157 serotypes.Microbiology (Reading, England) · 2011Article
- Analysis of RuvABC and RecG involvement in the escherichia coli response to the covalent topoisomerase-DNA complex.Journal of bacteriology · 2010Article
- Small molecule functional analogs of peptides that inhibit lambda site-specific recombination and bind Holliday junctions.Bioorganic & medicinal chemistry letters · 2010Article
- An antimicrobial peptide that targets DNA repair intermediates in vitro inhibits Salmonella growth within murine macrophages.Antimicrobial agents and chemotherapy · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Peptide inhibitors of phage lambda site-specific recombination were previously isolated by screening synthetic combinatorial peptide libraries. These inhibitors cause the accumulation of complexes between the recombinase and the Holliday junction intermediate of several highly divergent tyrosine recombinases. Peptide WRWYCR and its d-amino acid derivative bind to the center of protein-free junctions and prevent their resolution either by site-specific recombinases or by junction resolvases or helicases. With lesser affinity, the peptides also bind to branched DNA molecules that mimic replication forks. The peptides are bactericidal to both gram-positive and gram-negative bacteria, presumably because they can interfere with DNA repair and with chromosome dimer resolution by the XerC and XerD tyrosine recombinases. In order to test the correspondence between their mechanism in vivo and in vitro, we have tested and shown peptide wrwycr's ability to inhibit the excision of several prophages (lambda, P22, Gifsy-1, Gifsy-2, Fels-1, Fels-2) and to trap Holliday junction intermediates of phage lambda site-specific recombination in vivo. In addition, we found that the peptide inhibits replication of the Salmonella prophage Fels-1 while integrated in the chromosome. These findings further support the proposed mechanistic basis for the antimicrobial activity of the peptide and its use as a tool to dissect strand exchange-dependent DNA repair within cells.
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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.