ArticleJournal of bacteriology2014
The RimL transacetylase provides resistance to translation inhibitor microcin C.
Article in Journal of bacteriology, 2014. 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, 29 citations in OpenAlex.
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- Ribosomally Synthesized and Post-Translationally Modified Peptides Assembled by ThiF-like Adenylyltransferases: Recent Advances and Future Perspectives.Molecules (Basel, Switzerland) · 2025Review
- 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
- Whole genome sequencing distinguishes skin colonizing from infection-associatedFrontiers in cellular and infection microbiology · 2024Article
- Comparative Genomic Analysis of Shrimp-PathogenicMicroorganisms · 2023Article
- Engineering and Purification of Microcin C7 Variants Resistant to Trypsin and Analysis of Their Biological Activity.Antibiotics (Basel, Switzerland) · 2023Article
- Comparative analysis of the Colistin resistance-regulating gene cluster in Klebsiella species.Journal of microbiology (Seoul, Korea) · 2022Article
- Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu.The Journal of biological chemistry · 2022Article
- Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.International journal of molecular sciences · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020Review
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.The Journal of biological chemistry · 2019Review
- Microcins inFrontiers in microbiology · 2019Review
- Genome Features and Biochemical Characteristics of a Robust, Fast Growing and Naturally Transformable Cyanobacterium Synechococcus elongatus PCC 11801 Isolated from India.Scientific reports · 2018Article
- Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle.Nucleic acids research · 2018Article
- Article
- A Trojan-Horse Peptide-Carboxymethyl-Cytidine Antibiotic from Bacillus amyloliquefaciens.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
12 authors at 7 institutions in 3 countries.
Funding
Abstract
Peptide-nucleotide antibiotic microcin C (McC) is produced by some Escherichia coli strains. Inside a sensitive cell, McC is processed, releasing a nonhydrolyzable analog of aspartyl-adenylate, which inhibits aspartyl-tRNA synthetase. The product of mccE, a gene from the plasmid-borne McC biosynthetic cluster, acetylates processed McC, converting it into a nontoxic compound. MccE is homologous to chromosomally encoded acetyltransferases RimI, RimJ, and RimL, which acetylate, correspondingly, the N termini of ribosomal proteins S18, S5, and L12. Here, we show that E. coli RimL, but not other Rim acetyltransferases, provides a basal level of resistance to McC and various toxic nonhydrolyzable aminoacyl adenylates. RimL acts by acetylating processed McC, which along with ribosomal protein L12 should be considered a natural RimL substrate. When overproduced, RimL also makes cells resistant to albomycin, an antibiotic that upon intracellular processing gives rise to a seryl-thioribosyl pyrimidine that targets seryl-tRNA synthetase. We further show that E. coli YhhY, a protein related to Rim acetyltransferases but without a known function, is also able to detoxify several nonhydrolyzable aminoacyl adenylates but not processed McC. We propose that RimL and YhhY protect bacteria from various toxic aminoacyl nucleotides, either exogenous or those generated inside the cell during normal metabolism.
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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.