ArticleThe Journal of biological chemistry2010
The mechanism of microcin C resistance provided by the MccF peptidase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Ribosomally Synthesized and Post-Translationally Modified Peptides Assembled by ThiF-like Adenylyltransferases: Recent Advances and Future Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Article
- Microcin C7 as a Potential Antibacterial-Immunomodulatory Agent in the Postantibiotic Era: Overview of Its Bioactivity Aspects and Applications.International journal of molecular sciences · 2024Review
- Exploring the genetic basis of natural resistance to microcins.Microbial genomics · 2024Article
- Article
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
- Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.RSC chemical biology · 2021Review
- Modulation of Peptidoglycan Synthesis by Recycled Cell Wall Tetrapeptides.Cell reports · 2020Article
- Bacteriocins, Antimicrobial Peptides from Bacterial Origin: Overview of Their Biology and Their Impact against Multidrug-Resistant Bacteria.Microorganisms · 2020Review
- Article
- Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition.Nature communications · 2019Article
- Article
- Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by theChemical science · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Microcins inFrontiers in microbiology · 2019Review
- Peptide-nucleotide antibiotic Microcin C is a potent inducer of stringent response and persistence in both sensitive and producing cells.Molecular microbiology · 2017Article
- A Trojan-Horse Peptide-Carboxymethyl-Cytidine Antibiotic from Bacillus amyloliquefaciens.Journal of the American Chemical Society · 2016Article
- Article
- Structure and function of a novel LD-carboxypeptidase a involved in peptidoglycan recycling.Journal of bacteriology · 2013Article
- Article
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Authors and funding
9 authors.
Funding
Abstract
The heptapeptide-nucleotide microcin C (McC) is a potent inhibitor of enteric bacteria growth. Inside a sensitive cell, McC is processed by aminopeptidases, which release a nonhydrolyzable aspartyl-adenylate, a strong inhibitor of aspartyl-tRNA synthetase. The mccABCDE operon is sufficient for McC production and resistance of the producing cell to McC. An additional gene, mccF, which is adjacent to but not part of the mccABCDE operon, also provides resistance to exogenous McC. MccF is similar to Escherichia coli LdcA, an L,D-carboxypeptidase whose substrate is monomeric murotetrapeptide L-Ala-D-Glu-meso-A(2)pm-D-Ala or its UDP-activated murein precursor. The mechanism by which MccF provides McC resistance remained unknown. Here, we show that MccF detoxifies both intact and processed McC by cleaving an amide bond between the C-terminal aspartate and the nucleotide moiety. MccF also cleaves the same bond in nonhydrolyzable aminoacyl sulfamoyl adenosines containing aspartyl, glutamyl, and, to a lesser extent, seryl aminoacyl moieties but is ineffective against other aminoacyl adenylates.
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