ArticleFrontiers in microbiology2021
Multifaceted Mechanism of Amicoumacin A Inhibition of Bacterial Translation.
Article in Frontiers in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- A Microscale Platform for the Comprehensive Analysis of Bacterial Translation Initiation.International journal of molecular sciences · 2026Article
- Decoding the regulatory role of AmiC in amicoumacins production through transcriptomics and metabolic profiling in Bacillus subtilis fmb60.World journal of microbiology & biotechnology · 2026Article
- Article
- Characterization of the antagonistic secondary metabolites ofFrontiers in microbiology · 2025Article
- Isolation and characterization of an antimicrobial Bacillus subtilis strain O-741 against Vibrio parahaemolyticus.PloS one · 2024Article
- Structure and function of prodrug-activating peptidases.Biochimie · 2023Review
- Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.Nucleic acids research · 2023Article
- Biocontrol of fungal phytopathogens byFrontiers in microbiology · 2023Review
- Ψ-Footprinting approach for the identification of protein synthesis inhibitor producers.NAR genomics and bioinformatics · 2022Article
- A Biofloc-Based Aquaculture System Bio-augmented with Probiotic Bacteria Bacillus tequilensis AP BFT3 Improves Culture Environment, Production Performances, and Proteomic Changes in Penaeus vannamei.Probiotics and antimicrobial proteins · 2022Article
- AntimicrobialAntibiotics (Basel, Switzerland) · 2022Review
- Differential Contribution of Protein Factors and 70S Ribosome to Elongation.International journal of molecular sciences · 2021Article
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amicoumacin A (Ami) halts bacterial growth by inhibiting the ribosome during translation. The Ami binding site locates in the vicinity of the E-site codon of mRNA. However, Ami does not clash with mRNA, rather stabilizes it, which is relatively unusual and implies a unique way of translation inhibition. In this work, we performed a kinetic and thermodynamic investigation of Ami influence on the main steps of polypeptide synthesis. We show that Ami reduces the rate of the functional canonical 70S initiation complex (IC) formation by 30-fold. Additionally, our results indicate that Ami promotes the formation of erroneous 30S ICs; however, IF3 prevents them from progressing towards translation initiation. During early elongation steps, Ami does not compromise EF-Tu-dependent A-site binding or peptide bond formation. On the other hand, Ami reduces the rate of peptidyl-tRNA movement from the A to the P site and significantly decreases the amount of the ribosomes capable of polypeptide synthesis. Our data indicate that Ami progressively decreases the activity of translating ribosomes that may appear to be the main inhibitory mechanism of Ami. Indeed, the use of EF-G mutants that confer resistance to Ami (G542V, G581A, or ins544V) leads to a complete restoration of the ribosome functionality. It is possible that the changes in translocation induced by EF-G mutants compensate for the activity loss caused by Ami.
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