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Bordeaux, France
Joined February 2019
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Finding itself in this awkward position is more than just an inconvenience for the ribosome. It essentially disrupts everything it needs to catalyze peptide bond formation…
Teaming up with Thomas, Elodie biochemically and structurally characterized ribosomes translating QK motifs in the presence of TcmX, and found out that the drug traps the 3’ end of peptidyl-tRNA inside the exit tunnel with the help of the nascent peptide and the ribosome!
One of the drugs that caught Elodie and Thibaud's attention was TcmX, an aromatic polyketide that binds within the nascent polypeptide exit tunnel of the ribosome. It seems that TcmX allows the translation of most sequences, except those coding for a QK motif...
To determine whether this is indeed the case, Elodie used iTP-seq to study a large panel of drugs. iTP-seq is a tool developed in our lab that resembles Ribo-seq, but is performed in vitro, necessitates no prior knowledge of the translated sequences and requires fewer reads.
During translation, an almost infinite combination of nascent peptides, tRNAs and mRNAs transit through the ribosome. Since ribosome-targeting antibiotics must operate within this ever-changing setting, many of them are likely to be context-dependent inhibitors of translation.
A new study by @LeroyElodie3, Thomas Perry and @ThibaudRenault shows how the antibiotic Tetracenomycin X (TcmX) blocks translation of QK motifs by sequestering peptidyl-tRNA. @ERC_Research @iecb_bordeaux @arna_lab biorxiv.org/content/10.1101/…
The ribosome-arresting peptide TnaC captures a single L-Trp molecule to trigger the production of indole. Structures by @axvdstel and a great collaboration with the Cruz-Vera, Sachs and Mankin/Vazquez-Laslop @shuramankin labs! dlvr.it/RwnTSW
Our paper by @herrero_valle on ornithine sensing by the bacterial ribosome is finally out in @NatureMicrobiol! You can read it in its final version here: rdcu.be/b17qE.
