Many fundamental biochemical processes are governed by specific RNA/RNA and RNA/protein interactions. For example, RNA is involved in RNA cleavage (ribozymes and siRNA), regulation of translation (miRNA), RNA modification (snoRNA), and RNA splicing (snRNA). Even certain viruses carry their genomic material in the form of RNA, including the hepatitis C virus, which leads to chronic liver disease; the human immunodefiency virus (HIV) responsible of the Acquired Immuno-Deficiency Syndrome (AIDS); and the SARS-CoV a coronavirus responsible for the global outbreak of the Severe Acute Respiratory Syndrome (SARS).

Just like proteins, RNAs fold to form complex three-dimensional structures. The complexity in RNA function generally translates to the complexity of RNA structure. Our research focuses on NMR spectroscopic studies of RNA / RNA and RNA / protein complexes in order to gain a better structural understanding of RNA function. In addition, our research will bring new information on RNA structure and recognition, and this information will be useful in the design of drugs for the treatment of cancer and viral infections.

Although the main technique used for our studies is NMR spectroscopy, other biophysical methods (X-ray crystallography, UV spectroscopy, etc.) and biochemical studies are performed to complement the NMR studies. The research projects can be grouped along 4 main axes:

1. Structure, Function and Engineering of the Neurospora VS Ribozyme;
2. Structure and Function of Interactions Regulating the Human RNAPII CTD Phosphatase FCP1;
3. Structure of Viral RNAs and Proteins;
4. Functional Genomics and Drug Screening.

• Di Tomasso G, Miller Jenkins LM, Legault P. (2016) « ARiBo pull-down for riboproteomic studies based on label-free quantitative mass spectrometry » RNA. 22; 1760-1770.
• Lacroix-Labonté J, Girard N, Dagenais P, Legault P. (2016) « Rational engineering of the Neurospora VS ribozyme to allow substrate recognition via different kissing-loop interaction» Nucleic Acids Research, 44(14); 6924-6934.
• Bonneau, E., Girard, N, Lemieux, S. and Legault, P. (2015) « The NMR structure of the II-III-VI three-way junction from the Neurospora VS ribozyme reveals a critical tertiary interaction and provides new insight into the global ribozyme structure » RNA. 21; 1621-1632.
• Bouchard, P. and Legault P. (2014) « A remarkably stable kissing-loop interaction defines substrate recognition by the Neurospora Varkud Satelitte ribozyme »RNA. 20(9); 1451-1464.
• Desjardins, A., Bouvette, J. and Legault, P. (2014) « Stepwise assembly of multiple Lin28 proteins on the terminal loop of let-7 miRNA precursors » Nucleic Acids Research, 42(7); 4615-4628.
• Di Tomasso, G., Salvail-Lacoste, A. Bouvette, J. and Legault, P. (2014) « Affinity purification of in vitro transcribed RNA with homogenuous ends using a 3′-ARiBo tag » Methods in Enzymology Vol. 549: Riboswitch Discovery, Structure and Function.
• Bouchard, P. and Legault P. (2014) « Structural insights into substrate recognition by the Neurospora Varkud Satellite ribozyme: importance of U-turns at the kissing-loop junction » Biochemistry. 53(1); 258-269.
• Salvail-Lacoste, A., Di Tomasso G., Piette, B.L. and Legault P. (2013) « Affinity purification of T7 RNA transcripts with homogenous ends using ARiBo and CRISPR tags » RNA. 19(7): 1003-1014.
• Salvail-Lacoste, A., Di Tomasso G., Piette, B.L. and Legault P. (2013) « Affinity purification of T7 RNA transcripts with homogenous ends using ARiBo and CRISPR tags » RNA. 19(7): 1003-1014.
• Lacroix-Labonté, J., Girard, N., Lemieux, S. and Legault, P. (2012) « Helix-length compensation studies reveal the adaptability of the VS ribozyme architecture  » Nucleic Acids Research. 40(5): 2312-2329.
• Desjardins, A., Yang, A., Bouvette, J., Omichinski, J.G. and Legault, P. (2012) « Importance of the NCp7-like domain in the recognition of the let-7g precursor miRNA by the pluripotency factor Lin28 » Nucleic Acids Research. 40(4): 1767-1777.
• Di Tomasso, G., Lampron, P., Dagenais, P., Omichinski, J.G. and Legault, P. (2011) « The ARiBo tag: a reliable tool for affinity purification of RNAs under native conditions » Nucleic Acids Res. 39; 3 doi:10.1093/nar/gkp1084.
• Delfosse, V., Bouchard, P., Bonneau, E., Dagenais, P., Lemay, J.-F., Lafontaine, D. A., Legault, P. (2010) « Riboswitch structure: an internal residue mimicking the purine ligand » Nucleic Acids Res. 38(6); 2057-68