Our principal interest is to understand the fundamental aspect of protein synthesis mechanisms and regulations.

@ibpcF Paris, France
Joined February 2019
🚨👨‍🔬👩‍🔬 🚨 We are hiring: a 3-year postdoctoral position to study ABCF proteins in cyanobacteria. @IbpcF @EgmIbpc #postdocs #Paris #cyanobacteria #ribosome #ABCF
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We designed a motif that makes the expression of YFP strongly EttA-dependent. This motif demonstrates that EttA's activity is only evident when the motif is present within the first 30 amino acids of the encoded sequence.
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EttA-dependent regulation can be reversed—induced in the absence of EttA and repressed in its presence—by the use of a leader peptide like MgtL.
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EttA regulation allows E. coli to adapt to environmental changes by rerouting the TCA cycle via the glyoxylate shunt. Our study shows that this pathway, along with the tartronate-semialdehyde pathway, is crucial for adapting to salt stress.
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EttA rescues ribosomes that pause when repeats of acidic residues are present in the first 30 amino acids of the encoding sequences. These acidic residues can induce ribosomal stalling as well as abortive synthesis.
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Remind you of another translation factor? EttA and EF-P are different structurally, but in complex with the ribosome there is some similitude.
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Our model of the action of EttA.
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These regulatory activities are mediated by EttA rescuing ribosomes paused at specific patterns of negatively charged residues only within the first 30 amino acids of nascent proteins.
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EttA can also reduce gene expression using leader peptide to reverse the regulation.
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EttA directly controls the translation of mRNAs coding for a subset of enzymes in the tricarboxylic acid (TCA) cycle and its glyoxylate shunt, which dramatically modulates growth in some chemical environments. It also modulates expression of proteins involved and stress-response.
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