Matthew Smith, PhD

The overall focus of my research is to understand the mechanism of targeting and import of proteins into chloroplasts as a model for intracellular protein trafficking. We use a combination of molecular biology, biochemistry and biophysical approaches to understand the structural and functional details of the chloroplast protein import machinery.

• Faculty of Science Award for Teaching Excellence, Established Faculty category (2017).
• Natural Sciences and Engineering Research Council Discovery Accelerator Supplement recipient (2010).
• Early Researcher Award recipient from the Ontario Ministry of Economic Development and Innovation (2007).
• Canada Foundation for Innovation Leaders Opportunity Award recipient (2006).

I have on-going opportunities in my research lab for undergraduate and graduate students, and postdoctoral fellows, who are interested in cell biology, plant biology, molecular biology, and protein biochemistry research.

Tabefam, M., Smith, M.D.* and Jelokhani-Niaraki, M.*. 2024. Expression, purification and folding of native like mitochondrial carrier proteins in lipid membranes. Frontiers in Biophysics, 1: 1334804. https://doi.org/10.3389/frbis.2023.1334804. *Co-corresponding authors

Fish, M., Nash, D., Germanu, A., Overton, A., Jelokhani-Niaraki, M., Chuong, S.D.X. and Smith, M.D. 2022. New insights into the chloroplast outer membrane proteome and associated targeting pathways. International Journal of Molecular Sciences, 23(3): 1571. doi: 10.3390/ijms23031571

Ardalan, A., Smith, M.D. and Jelokhani-Niaraki, M. 2022. Uncoupling proteins and regulated proton leak in mitochondria. International Journal of Molecular Sciences, 23(3): 1528. doi: 10.3390/ijms23031528

Ardalan, A., Sowlati-Hashjin, S., Oduwoye, H., Uwumarenogie, S., Karttunen, M., Smith, M.D. and Jelokhani-Niaraki, M. 2021. Biphasic proton transport mechanism for Uncoupling Proteins. Journal of Physical Chemistry B, 125 (32): 9130-9144. doi: 10.1021/acs.jpcb.1c04766

Ardalan, A., Sowlati-Hashjin, S., Uwumarenogie, S.O., Fish, M., Mitchell, J., Karttunen, M., Smith, M.D. and Jelokhani-Niaraki, M. 2021. Functional oligomeric forms of uncoupling protein 2: strong evidence for asymmetry in protein and lipid bilayer systems. The Journal of Physical Chemistry, Part B: Biophysics, Biomaterials, Liquids, Soft Matter; Section B: Biomaterials and Membranes, 125 (1): 169-183. doi: 10.1021/acs.jpcb.0c09422

Teresinski, H.J., Gidda, S.K., Nguyen, T.N.D., Marty-Howard, N.J., Porter, B.K., Grimberg, N., Smith, M.D., Andrews, D.W., Dyer, J.M. and Mullen, R.T. 2019. An RK/ST C-terminal motif is required for targeting of OEP7.2 and a subset of other Arabidopsis tail-anchored proteins to the plastid outer envelope membrane. Plant and Cell Physiology, 60(3): 516-537. doi: 10.1093/pcp/pcy234

Hoang, T., Kuljanin, M., Smith, M.D. and Jelokhani-Niaraki, M. 2015. A study on molecular physiology of the uncoupling proteins of the central nervous system. Bioscience Reports, 35(4): e00226. doi: 10.1042/BSR20150130

Hoang, T., Matovic, T., Parker, J., Smith, M.D. and Jelokhani-Niaraki, M. 2015. Role of positively charged residues of the second transmembrane domain in the ion transport activity and conformation of human uncoupling protein-2. Biochemistry, 15(14): 2303-2313. doi: 10.1021/acs.biochem.5b00177

Lung, S.-C., Smith, M.D. and Chuong, S.D.X. 2015. Isolation of chloroplasts from plant protoplasts. In, Subcellular Fractionation: A Laboratory Manual, P. Pryor, Ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Chapter 14, pp. 159-163.

Campbell, J.H., Hoang, T., Jelokhani-Niaraki, M. and Smith, M.D. 2014. Folding and self-association of atTic20 in lipid membranes: implications for understanding protein transport across the inner envelope membrane of chloroplasts. BMC Biochemistry, 15:462. doi: 10.1186/s12858-014-0029-y

Lung, S.-C., Gwynne, W., Secord, N., Weston, J.K., Smith, M.D. and Chuong, S.D.X. 2014. The C-terminus of Bienertia sinuspersici Toc159 contains essential elements for targeting to the chloroplast outer membrane. Frontiers in Plant Science, 5:722. doi: 10.3389/fpls.2014.00722

Richardson, L.G., Paila, Y., Siman, S., Chen, Y., Smith, M.D. and Schnell, D.J. 2014. Targeting and Assembly of Components of the TOC Protein Import Complex at the Chloroplast Outer Envelope Membrane. Frontiers in Plant Science, 5:269. doi: 10.3389/fpls.2014.00269.

Yan, J., Campbell, J., Glick, B.R., Smith, M.D.* and Liang, Y*. 2014. Molecular Characterization and Expression Analysis of Chloroplast Protein Import Components in Tomato (Solanum lycopersicum). PLoS ONE, 9(4): e94088. doi: 10.1371/journal.pone.0095088 *co-corresponding authors.

Dutta, S., Teresinski, H. and Smith, M.D. 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

Hoang, T., Smith. M.D. and Jelokhani-Niaraki, M. 2013. Expression, folding and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: evidence for associated functional forms. Journal of Biological Chemistry, 288(51): 36244-36258. doi: 10.1074/jbc.M113.509935

Hoang, T., Smith. M.D. and Jelokhani-Niaraki, M. 2012. Towards understanding the mechanism of ion transport activity of neuronal uncoupling proteins – UCP2, UCP4 and UCP5. Biochemistry, 51, 4004-4014. doi: 10.1021/bi3003378

Smith, M.D and Jelokhani-Niaraki, M. 2012. pH-induced changes in intrinsically disordered proteins. In, Methods in Molecular Biology Series #896: Intrinsically Disordered Protein Analysis, Vol. 2, Methods and Experimental Tools. V.N. Uversky & A.K. Dunker, Eds. Pgs. 223-231. Springer Protocols, Humana Press.

Dhanoa, P.K., Richardson, L.G.L., Smith, M.D. Gidda, S.K., Henderson, M.P.A., Andrews, D.W. and Mullen, R.T. 2010. Distinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope. PLoS ONE, 5(4): e10098. doi: 10.1371/journal.pone.0010098

Richardson, L.G.L., Jelokhani-Niaraki, M. and Smith, M.D. 2009. The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. BMC Biochemistry, 10:35. doi: 10.1186/1471-2091-10-35

Smith, M.D. 2006. Protein import into chloroplasts: an ever-evolving story. Can J Bot, 84: 531-542

Tu, S.-L., Chen, L.-J., Smith, M.D., Su, Y.-s., Schnell, D.J. and Li, H.-m. 2004. Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75. The Plant Cell, 16: 2078-2088. doi: https://doi.org/10.1105/tpc.104.023952

Ivanova, Y.G.1, Smith, M.D.1, Chen, K. and Schnell, D.J. 2004. Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids. Molecular Biology of the Cell, 15: 3379-3392 (1authors contributed equally to the work) doi: 10.1091/mbc.e03-12-0923

Smith, M.D., Rounds, C.M., Wang, F., Chen, K., Afitlhile, M. and Schnell, D.J. 2004. atToc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins. J Cell Biol, 165: 323-334 doi: 10.1083/jcb.200311074

Recent Undergraduate Courses:

• BI110 - Unifying Life Processes
• BI338 - Cells: Form and Function
• BI346 - Advanced Molecular Biology
• BI441 - Recombinant DNA Technology

• Laurier opens new rooftop research greenhouse as part of open doors 2015 event.