Strathcona Anatomy & Dentistry Building
3640 University Street
Structure and function of macromolecular machines using high-resolution molecular electron microscopy.
Cryo-electron microscopy and cryo-electron tomography are powerful imaging techniques that are ideally suited for the study of large and complex molecular machines in their dynamic state as well as for the investigation of complex cellular events. These techniques allow the study of the conformational changes that a given molecular complex undergoes during its physiological pathway (in its fully hydrated state and in the presence of membranes if necessary). They are unique tools in cell biology to understand the relationship between structure and function of macromolecules and organelles. The three dimension electron density maps calculated from these techniques can be used to computationally dock high resolution data (obtained by x-ray or NMR) of the individual components of the complex.
Cellular membranes allow life forms to exist. They serve as a barrier to the external environment and organize the interior of the eukaryotic cell into biochemically distinct compartments in which specific cellular functions are performed. Transport of proteins in between the cellular compartment (tubular or vesicular transport) and across the cellular membranes (translocation) as well as membrane dynamic (fusion and fission) are often driven and controlled by macromolecular complexes. Our laboratory is particularly interested in studying these processes using a structure-function type of approach with high-resolution molecular electron microscopy as the structural technique. Specific interests of the laboratory are entry of anthrax toxins in the cell, entry of polyomavirus in the cell, role of p97 in ERAD, function of OPA1/Drp1 in mitochondria fusion and fission… and more.
For more information on the research in the laboratory, please visit our website.
Alisaraie L, Rouiller I.
Full-length structural model of RET3 and SEC21 in COPI: identification of binding sites on the appendage for accessory protein recruitment motifs. J Mol Model. 2012 Jan 14. [Epub ahead of print]
Xu XP, Rouiller I, Slaughter BD, Egile C, Kim E, Unruh JR, Fan X, Pollard TD, Li R, Hanein D, Volkmann N.
Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors. EMBO J. 2011 Sep 20;31(1):236-47. doi: 10.1038/emboj.2011.343.
Zhang T, Dayanandan B, Rouiller I, Lawrence EJ, Mandato CA.
Growth-arrest-specific protein 2 inhibits cell division in Xenopus embryos. PLoS One. 2011;6(9):e24698. Epub 2011 Sep 9.
Song W, Chen J, Petrilli A, Liot G, Klinglmayr E, Zhou Y, Poquiz P, Tjong J, Pouladi MA, Hayden MR, Masliah E, Ellisman M, Rouiller I, Schwarzenbacher R, Bossy B, Perkins G, Bossy-Wetzel E.
Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat Med. 2011 Mar;17(3):377-82. Epub 2011 Feb 20.
Karam P, Ngo AT, Rouiller I, Cosa G.
Unraveling electronic energy transfer in single conjugated polyelectrolytes encapsulated in lipid vesicles. Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17480-5. Epub 2010 Sep 27.
Byrne ME, Ball DA, Guerquin-Kern JL, Rouiller I, Wu TD, Downing KH, Vali H, Komeili A.
Desulfovibrio magneticus RS-1 contains an iron- and phosphorus-rich organelle distinct from its bullet-shaped magnetosomes. Proc Natl Acad Sci U S A. 2010 Jul 6;107(27):12263-8. Epub 2010 Jun 21.
Yu S, Azzam T, Rouiller I, Eisenberg A.
"Breathing" vesicles. J Am Chem Soc. 2009 Aug 5;131(30):10557-66.