%0 Unpublished work %T Queuosine modification of tRNA-Tyrosine elicits translational reprogramming and enhances growth of Vibrio cholerae with aminoglycosides %+ Plasticité du Génome Bactérien - Bacterial Genome Plasticity (PGB) %+ Hub Bioinformatique et Biostatistique - Bioinformatics and Biostatistics HUB %+ Plateforme de Protéomique / Proteomics platform %+ Chimie biologique épigénétique - Epigenetic Chemical Biology (EpiCBio) %+ Institut de Biologie Intégrative de la Cellule (I2BC) %+ Department of Microbiology and Cell Science %+ University of Florida Genetics Institute (UFGI) %A Fruchard, Louna %A Babosan, Anamaria %A Carvalho, Andre %A Lang, Manon %A Li, Blaise %A Duchateau, Magalie %A Giai-Gianetto, Quentin %A Matondo, Mariette %A Bonhomme, Frédéric %A Fabret, Céline %A Namy, Olivier %A de Crécy-Lagard, Valérie %A Mazel, Didier %A Baharoglu, Zeynep %Z This research was funded by the Institut Pasteur, the Centre National de la Recherche Scientifique (CNRS-UMR 3525), ANR ModRNAntibio (ANR-21-CE35-0012), ANR-LabEx [ANR-10-LABX-62-IBEID], the Fondation pour la Recherche Médicale (FRM EQU202103012569), the Institut Pasteur grant PTR 245-19 and by the National Institute of General Medical Sciences (NIGMS) grant GM70641 to V dC-L. AB was funded by Institut Pasteur Roux-Cantarini fellowship. The authors acknowledge a DIM1Health 2019 grant from the Région Ile de France to the project EpiK for the LCMS equipment. %8 2023-05-10 %D 2023 %R 10.1101/2022.09.26.509455 %Z Life Sciences [q-bio]Preprints, Working Papers, ... %X Tgt is the enzyme modifying the guanine (G) in tRNAs with GUN anti-codon to queuosine (Q). tgt is required for optimal growth of Vibrio cholerae in the presence of sub-lethal aminoglycoside concentrations. We further explored here the role of the Q 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 Q modification in antibiotic translational stress response. Using molecular reporters, we showed that Q 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 tgt . RsxA displays a codon bias towards tyrosine TAT and its overabundance leads to decreased expression of genes belonging to SoxR oxidative stress regulon. We also identified conditions that regulate tgt expression. We propose that regulation of Q modification in response to environmental cues leads to translational reprogramming of genes bearing a biased tyrosine codon usage. In silico analysis further identified candidate genes possibly subject to such translational regulation, among which DNA repair factors. Such transcripts, fitting the definition of modification tunable transcripts, are plausibly central in the bacterial response to antibiotics. %G English %2 https://pasteur.hal.science/pasteur-04093412/document %2 https://pasteur.hal.science/pasteur-04093412/file/2022.09.26.509455.full.pdf %L pasteur-04093412 %U https://pasteur.hal.science/pasteur-04093412 %~ PASTEUR %~ CEA %~ CNRS %~ INC-CNRS %~ CEA-UPSAY %~ I2BC %~ UNIV-PARIS-SACLAY %~ JOLIOT %~ CEA-DRF %~ UNIV-PARIS %~ UNIVERSITE-PARIS %~ UNIVERSITE-PARIS-SACLAY %~ ANR %~ GS-BIOSPHERA %~ GS-LIFE-SCIENCES-HEALTH %~ GS-HEALTH-DRUG-SCIENCES %~ TEST2-HALCNRS %~ FRM %~ BACTERIAL-GENOME-PLASTICITY %~ UMR3525 %~ FRANCE-GENOMIQUE %~ BIOMICS_IP %~ BIOINFO_BIOSTAT_HUB