Our research group focuses on advancing knowledge of structure-function relationships in enzymes to facilitate enzyme modification for specific purposes. Enzyme modification is a growing field in response to policies promoting environmentally friendly catalysts. Our approach involves combinatorial mutagenesis of enzyme active sites, selecting enzymes through accelerated evolution, and characterizing them using kinetic and structural analyses, as well as computer-assisted molecular modeling. Our work also aims to better understand enzyme-induced drug resistance in the health sciences sector. Our interdisciplinary work in bio-organic chemistry, biochemistry, and bioinformatics contributes to the development of modern enzymology.
Transglutaminases catalyze the cross-linking of proteins, by binding an amine (a lysine bound to a protein or peptide) to the terminal amide of a glutamine bound to a protein or peptide. Transglutaminases are increasingly used in protein labeling systems, where various amino compounds are bound to proteins, giving the modified proteins new properties.
Cytochromes P450 oxidize hydrophobic compounds to increase an organism's ability to eliminate these compounds. The oxidation reactions they catalyze have great potential for biocatalytic applications. To this end, we are experimentally adapting the Bacillus megaterium cytochrome P450 to catalyze industrially relevant reactions.
Dihydrofolate reductases (Dfr) are essential for cell proliferation. Therefore, they are the target of the antibiotic trimethoprim. The emergence of an alternative Dfr, Dfr type B (DfrB), confers insurmountable resistance to trimethoprim. We investigate the evolution and function of this enzyme by combining bioinformatics and experimental methods to inform our design of DfrB-specific inhibitors.
In collaboration with the research laboratories of Jean-François Masson (U. of Montreal) and Denis Boudreau (U. Laval), with the help of organizations such as Instruments Scientifiques Affinité, Héma-Québec and many other collaborators, we are currently developing a combined ELISA and SPR (Surface Plasmon Resonance) approach to quantify and characterize antibodies against SARS-CoV-2.
Claudèle Lemay-St-Denis, one of our PhD students, was featured in a comic about her graduate studies at Université de Montréal. Read the comic here: https://mtlphd.com/2022/09/20/claudele-doctorante-en-biochimie/.
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Stella Cellier-Goetghebeur, one of our PhD students, won a science communication prize for the article she published in 'DIRE', the popular science magazine in which articles written by graduate students at the University of Montreal are published.
'A conserved SH3-like fold in diverse putative proteins tetramerizes [...]' was published in Philosophical Transactions of the Royal Society B.
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'Epistasis between promoter activity and coding mutations shapes gene evolvability' was published in Science Advances, in collaboration with the Landry laboratory (U. Laval).
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'From a binding module to essential catalytic activity: how nature stumbled on a good thing', a review of the DfrB project was published in Chemical Communications.
'Tag-free, specific conjugation of glycosylated IgG1 antibodies using microbial transglutaminase' was published in RSC Advances.
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'Assessment of the longitudinal humoral response in non-hospitalized SARS-CoV-2-positive individuals [...]' was published in Frontiers in Immunology.
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'Tuning Selectivity in CalA Lipase: Beyond Tunnel Engineering' was published in Biochemistry.
The Joelle Pelletier laboratory is pleased to welcome one new employees: Douglas Fansher (post-doc) as well as two new PhD students: Samy Faraj and Alexis Bonneau-Burke.
ADRESSE / ADDRESS
Université de Montréal
Département de Chimie
Campus MIL - Local B-6227
1375 Ave.Thérèse-Lavoie-Roux
Montreal, Qc, Canada, H2V 0B3
CONTACT
Phone: +1 (514) 343-2124
Fax: +1 (514) 343-7586
@ : joelle.pelletier@umontreal.ca