Moira Glerum

Moira Glerum
Location: QNC 3623
Phone: 519-888-4567 x31352


Mitochondria are essential energy generators in almost all eukaryotic cell and defects in mitochondrial structure and function have been identified in a wide variety of human diseases. In fact, defects in mitochondrial function may be the most common underlying cause of neurodegenerative disease! Mitochondria are comprised of proteins encoded in two different genomes - the nuclear (nDNA) and the mitochondrial (mtDNA). The Glerum lab is studying the contributions of both of these genomes to neurodegenerative diseases and cancer.

The nuclear genome encodes most of the proteins required for mitochondrial formation. One of the key enzymes found in mitochondria is cytochrome oxidase (COX), which consists of 13 subunits - 3 encoded in mtDNA and 10 encoded in the nucleus. In addition, there are some two dozen proteins involved in ensuring that COX is correctly assembled, all of which are also encoded in the nDNA. The COX assembly pathway is most often defective in human COX deficiencies, which are the most common of the mitochondrial respiratory chain disorders. These diseases usually present early in life and are almost always fatal. The COX assembly pathway is still only partially understood and we are using yeast as a model system for delineating this process. Our studies are furthering our understanding of how mutations in COX assembly genes result in fatal neurological disease.

Microfluidic chip, or lab-on-a-chip, technologies have the potential to revolutionize both health care delivery and biomedical research. Given the ever-increasing list of disorders with a documented mitochondrial dysfunction, technologies that would enable us to investigate mitochondrial function at the level of a single cell would further our understanding of the contributions of this organelle to disease pathologies. In collaboration with the Backhouse lab in Electrical and Computer Engineering, we are therefore also developing microfluidic chip-based assays for use in studying mitochondrial disease.

Research Interests

  • Physiology, Cell and Developmental Biology
  • Molecular Genetics


  • 1990 Ph.D. Biochemistry, University of Toronto, Canada
  • 1984 B.Sc. Biochemistry, University of Toronto, Canada


  • 2015 Jack Carlson Teaching Award, Department of Biology
  • 2003-2010 Senior Scholar, Alberta Heritage Foundation for Medical Research
  • 2001-2002 Scholar, Canadian Genetic Diseases Network
  • 1998-2003 New Investigator, Canadian Institutes of Health Research
  • 1998-2003 Scholar, Alberta Heritage Foundation for Medical Research
  • 1994-1997 Postdoctoral Fellowship, Medical Research Council of Canada
  • 1989 David F. Scott Award, Department of Biochemistry, University of Toronto
  • 1984-1988 Doctoral Fellowship, Hospital for Sick Children Research Institute

Professional Associations

  • American Society for Microbiology
  • American Society for Biochemistry and Molecular Biology
  • Canadian Society of Molecular BioSciences

Affiliations and Volunteer Work

  • Waterloo Institute for Nanotechnology
  • Waterloo Centre for Microbial Research


  • BIOL 331 - Advanced Cell Biology
    • Taught in 2018, 2019, 2020, 2021
  • BIOL 472 - Cell Biology of Human Disease
    • Taught in 2018, 2020
  • NE 381 - Introduction to Nanoscale Biosystems
    • Taught in 2018

* Only courses taught in the past 5 years are displayed.

Selected/Recent Publications

  • Hall, G.H., Glerum, D.M., Backhouse, C.J. (2016) A light emitting diode, photodiode-based detection system for DNA analysis with microchip electrophoresis. Electrophoresis 37, 406-413.
  • Hall, G.H., Sloan, D., Ma, T., Couse, M.H., Martel, S., Elliott, D.G., Glerum, D.M., Backhouse, C.J. (2014) An optical relay approach to very low cost hybrid polymer-CMOS electrophoresis instrumentation. J. Chrom. A 1349, 122-128.
  • Veniamin, S., Sawatzky, L.G., Banting, G., Glerum, D.M. (2011) Characterization of the peroxide sensitivity of COX deficient yeast strains reveals unexpected relationships between COX assembly proteins. Free Radic. Biol. Med. 51, 1589-1600.