Fiche publication
Date publication
janvier 2025
Journal
eLife
Auteurs
Membres identifiés du Cancéropôle Est :
Pr MOTORINE Iouri
,
Dr MARCHAND Virginie
Tous les auteurs :
Fruchard L, Babosan A, Carvalho A, Lang M, Li B, Duchateau M, Giai Gianetto Q, Matondo M, Bonhomme F, Hatin I, Arbes H, Fabret C, Corler E, Sanchez G, Marchand V, Motorin Y, Namy O, de Crécy-Lagard V, Mazel D, Baharoglu Z
Lien Pubmed
Résumé
Tgt is the enzyme modifying the guanine (G) in tRNAs with GUN anticodon to queuosine (Q). is required for optimal growth of in the presence of sub-lethal aminoglycoside concentrations. We further explored here the role of the Q34 in the efficiency of codon decoding upon tobramycin exposure. We characterized its impact on the overall bacterial proteome, and elucidated the molecular mechanisms underlying the effects of Q34 modification in antibiotic translational stress response. Using molecular reporters, we showed that Q34 impacts the efficiency of decoding at tyrosine TAT and TAC codons. Proteomics analyses revealed that the anti-SoxR factor RsxA is better translated in the absence of . RsxA displays a codon bias toward tyrosine TAT and overabundance of RsxA leads to decreased expression of genes belonging to SoxR oxidative stress regulon. We also identified conditions that regulate expression. We propose that regulation of Q34 modification in response to environmental cues leads to translational reprogramming of transcripts bearing a biased tyrosine codon usage. In silico analysis further identified candidate genes which could be subject to such translational regulation, among which DNA repair factors. Such transcripts, fitting the definition of modification tunable transcripts, are central in the bacterial response to antibiotics.
Mots clés
Vibrio cholerae, antibiotic stress, epitranscriptome, genetics, genomics, infectious disease, microbiology, post-transcriptional regulation, queuosine, tRNA modification
Référence
Elife. 2025 01 6;13:
