John R. Glover

John R. Glover

Associate Professor

BSc, University of Guelph, 1981-1984
MSc, University of Guelph, 1985-1987
PhD, McMaster University, 1990-1994
Postdoc, HHMI University of Chicago, 1994-1998

Address Rm 1616 MaRS West Tower
Toronto, ON M5S 1A8
Office Phone 416-200-5985

I was raised on a farm in southern Ontario. During high school I became passionately interested in playing and performing music and pursued that passion for ten years. After a fairly successful run I was ready to continue my education and went to the University of Guelph to take agriculture with the idea of going home and running the family farm. During my undergrad a had opportunities to get some practical research experience and found that I had a passion for molecules. I finished my agriculture degree and then did an MSc in plant biochemistry, a PhD in yeast molecular genetics and cell biology working on peroxisome biogenesis at McMaster University, and finally did a postdoc at the HHMI, University of Chicago with Dr. Susan Lindquist.

As a PhD student I discovered that proteins synthesized and the cytoplasm are translocated through the peroxisomal membrane as fully-folded and assemble oligomers. How this can happen without compromising the integrity of the membrane barrier is still an open question. As a postdoc I worked on reconstitution of the activity of the molecular chaperone Hsp104 and discovered that this protein worked together with the Hsp70 molecular chaperones to resolubilize and refold denatured, aggregated proteins. More recently, in collaboration with Lewis Kay and talented postdoc Rina Rosenzweig, we solved the mystery of how Hsp70 interacts with Hsp104. I also played a important role in demonstrating certain proteins in yeast can adopt a self-replicating, amyloid-like conformation. The amyloid particles that serve protein-only inherited elements or “propagons” are generated by the action of Hsp104.

In addition to research and teaching, I organize the Sumer Student Enrichment Program in Biochemistry (SSEPB). SSEPB is an inspiring series in which young people with advanced biochemistry degrees with diverse careers are invited to tell students how they navigated the transition from school to work.

In my spare time I enjoy playing guitar and writing songs. For many years I and my colleague, Dr. David Williams, have been called upon to compose parody songs for Holiday parties and other special occasions around the department.

Research Lab

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Research Description

Protein Aggregation

Proteins are made up of long strings of building blocks called amino acids. But rather than existing as extended or random arrangements, most proteins fold up into well-ordered structures. The order of the building blocks that make up the protein string is different for each protein and it is this sequence of amino acids that determines exactly how the protein folds under ideal conditions. However under non-ideal conditions or when a genetic mutation causes the amino acid sequence to change, proteins may fail to fold correctly and these misfolded protein tend be sticky and become tangled up with other misfolded proteins. These proteins are physically trapped and almost impossible to separate easily.

Protein aggregates are characteristic of serious human diseases such as Alzheimer’s or Parkinson’s Disease, might be toxic, and result in cell death. When yeast proteins aggregate – and some of these aggregates are surprisingly like those that cause human disease – the protein we study performs the task of unraveling the tangled ball, extracting out single strings of amino acids and helping them refolded in the correct manner. By understanding how Hsp104 works we hope to learn about protein aggregation and how damaged cells can be encouraged to dissolve aggregates more efficiently in hopes of eventually being able to cure a range of diseases.

origami crane


View all publications on PubMed

Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.
Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE.
Science. 2013 Mar 1;339(6123):1080-3

Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).
Helsen CW, Glover JR
J Biol Chem. 2012 Jan 2;287(1):542-56

Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding.
Lum R, Niggemann M, Glover JR.
J Biol Chem. 2008 Oct 31;283(44):30139-50

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.
Lum R, Tkach JM, Vierling E, Glover JR.
J Biol Chem. 2004 Jul 9;279(28):29139-46