Our main research projects focus on the study of translation initiation in eukaryotes. We research and study unconventional initiation mechanisms that use structural elements of mRNA to recruit initiation factors and ribosomes. One model system is the mouse histone H4 mRNA for which we have characterized a novel initiation mechanism based on internal ribosome entry from initiation factors attached to secondary mRNA structures. The laboratory is also interested in the IRES (internal ribosome entry site) of the Cricket Paralysis Virus (CrPV) and the mechanism of initiation and translational recoding of selenoprotein mRNAs.
Aminoacyl-tRNA synthetases form a family of enzymes that catalyze the esterification of amino acids on the 3′ end of transfer RNAs (tRNAs). Since the classification of aminoacyl-tRNA synthetases into two distinct classes, established in 1990 in the laboratory, our team has carefully dissected the functioning of 2 model enzymes which are aspartyl-tRNA synthetase and arginyl-tRNA synthetase, class II and I enzymes respectively. Our studies also focused on the correction or editing reaction catalyzed by aminoacyl-tRNA synthetases. This essential step helps to verify and correct aminoacylation products by hydrolyzing them before or after their transfer to tRNAs.
Our investigative techniques include molecular biology, biochemistry, cell biology, chemical and enzymatic surveys, SHAPE, bacterial genetics, yeast genetics, enzymology, electron microscopy and radiocrystallography.