Dr. Matthew Smith
Associate Professor, Biology; Associate Dean, Postdoctoral Affairs, Faculty of Graduate and Postdoctoral Studies
Contact InformationEmail: email@example.com
Phone: 519-884-0710 ext.2916 | lab 519-884-0710 ext.2176
Office Location: N3021J
Office Hours: By appointment
Academic BackgroundPostdoctoral Training: Molecular Plant Cell Biology and Biochemistry, University of Massachusetts, Amherst, USA (2000-04)
PhD: Biology, University of Waterloo (2000)
BSc: Honours Biology, Wilfrid Laurier University (1995)
Area of Research: Mechanisms of protein targeting and import into chloroplasts
Selected Publications (see "Research Publications" section for selected PDFs):
S. Dutta, H. Teresinski, and M.D. Smith. 2014. A split-ubiquitin yeast two-hybrid screen to examine the substrate specificity of atToc159 and atToc132, two Arabidopsis chloroplast preprotein import receptors. PLoS ONE, 9(4): e95026. doi:10.1371/journal.pone.0095026.
M. Ivanova, T. Hoang, F.R. McSorley, G. Krnac, M.D. Smith and M. Jelokhani-Niaraki. 2010. A comparative study on conformation and ligand binding of the neuronal uncoupling proteins. Biochemistry, doi:10.1021/bi901742g.
L.G.L. Richardson, M. Jelokhani-Niaraki and M.D. Smith. 2009. The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. BMC Biochem, 10:35.
A.K. Padham, M.T. Hopkins, T.-W. Wang, L.M. Nowack, M. Lo, L. Richardson, M.D. Smith, C.A. Taylor and J.E. Thompson. 2007. Characterization of a plastid triacylglycerol lipase from Arabidopsis. Plant Physiol, 143: 1372-1384.
M. Jelokhani-Niaraki, M. Ivanova, B.L. McIntyre, C.L. Newman, F.R. McSorley, E.K. Young and M.D. Smith. 2008. A circular dichroism study of uncoupling protein-1 and its transmembrane and matrix-loop domains. Biochem J, 411: 593-603.
M.D. Smith. 2006. Protein import into chloroplasts: an ever-evolving story. Can J Bot, 84: 531-542
M.D. Smith and D.J. Schnell. 2004. Chloroplast protein targeting: multiple pathways for a complex organelle. In Protein movement across membranes. J. Eichler, ed., Landes Bioscience,
Y.G. Ivanova*, M.D. Smith*, K. Chen, and D.J. Schnell. 2004. Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids. Mol Biol Cell, 15: 3379-3392 (*These authors contributed equally to this work).
M.D. Smith, C.M. Rounds, F. Wang, K. Chen, M. Afitlhile and D.J. Schnell. 2004. atToc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins. J Cell Biol, 165 (3): 323-334.
T.R. Wallas, M.D. Smith, S. Sanchez-Nieto and D.J. Schnell. 2003. The roles of Toc34 and Toc75 in targeting the Toc159 preprotein receptor to chloroplasts. J Biol Chem, 278 (45): 44289-44297.
M.D. Smith, A. Hiltbrunner, F. Kessler and D.J. Schnell. 2002. The targeting of the atToc159 preprotein receptor to the chloroplast outer membrane is mediated by its GTPase domain and is regulated by GTP. J Cell Biol, 159: 833-843.
M.D. Smith, L. Fitzpatrick, K. Keegstra and D.J. Schnell. 2002. In vitro analysis of chloroplast protein import. Curr Prot Cell Biol, Supplement 14: 11.16.1-11.16.21 (Invited methods chapter).
M.D. Smith and D.J. Schnell. 2001. Peroxisomal protein import: the paradigm shifts. Cell, 105: 293-296 (Invited Minireview).