Dr. Dale Cameron
Dr. Dale Cameron

Dale Cameron

Our research focuses on prions – proteins that can switch into alternative structures and then convert normal copies of the same protein into these alternative structures. Using yeast cells as our model, we want to understand how prion formation is triggered, and the impact of prion formation on cell fitness in different environments.

Dale Cameron joined the Ursinus College faculty in 2009.  Originally from Australia, Dale received his Bachelor of Science in Molecular Genetics and his PhD in Biochemistry and Molecular Genetics from the University of New South Wales in Sydney. He carried out his graduate work on protein synthesis with Dr. Paul March at UNSW and with Dr. Albert Dahlberg as a visiting research scholar at Brown University.  Dale was a postdoctoral fellow in the lab of Dr. Jonathan Weissman at the University of California in San Francisco, where he began to use the yeast Saccharomyces cereviseae as a model system.

The Cameron lab studies the role of protein misfolding and aggregation in both normal biology and disease states using yeast as a model organism. Proteins carry out many different tasks in cells, but in order to be functional each protein must first fold into the correct three dimensional structure. Most proteins are able to fold into multiple conformations, and ensuring each protein adopts the correct structure is an important challenge for cells. Misfolded proteins cannot carry out their normal functions and may sometimes even take on new, potentially toxic functions. Prions (“pree-ons”) are a very unique class of misfolded proteins because their misshapen aggregation-prone conformation can replicate and propagate infectiously. Prions are the cause of diseases like “mad cow” disease, scrapie in sheep, chronic wasting disease in deer and elk, and Creutzfeldt-Jakob disease in humans. 

The Cameron lab uses a combination of genetics, cell biology and biochemistry to address several broad questions related to protein misfolding and aggregation. What is the role of protein aggregation in normal biology and how does this phenomenon affect cellular physiology? Why do prions exist? How do cells protect themselves from the potentially toxic consequences of expressing aggregation-prone proteins? His work has been funded by grants from the Research Corporation for Science Advancement and the National Institutes of Health.




  • B.Sc.(Hons), University of New South Wales
  • Ph.D., University of New South Wales


BIO102 Cell Biology (Lecture and Lab)
BIO201 Genetics (Lecture and Lab)
BIO328 Protein Biogenesis (Lecture and Lab)
BIO428W Genomics
CIE200 Common Intellectual Experience

Research Interests

Protein synthesis and protein misfolding; self-propagating protein conformations (prions)
Mechanisms regulating prion formation in yeast
Physiological consequences of yeast prions
Positive and negative impacts of prion formation on yeast fitness and survival

Recent Work

Kelly C, Ahmed Y, Elghawy O, Pachon NF, Fontanese MS, Kim S, Kitterman E, Marley A, Terrenzio D, Wike R, Zeibekis T, Cameron DM*. The human ribosome-associated complex suppresses prion formation in yeast. Proteins. 2023 Jan 5. doi: 10.1002/prot.26461. Epub ahead of print. PMID: 36604744. (view full text)
(Undergraduate student collaborators are bolded)
* Corresponding author

Allwein B, Kelly C, Kammoonah S, Mayor T, Cameron DM*. Prion-dependent proteome remodeling in response to environmental stress is modulated by prion variant and genetic background. (2019). Prion 13, 53-64 (view full text)
(Undergraduate student collaborators are bolded)   * Corresponding author

Chan PHW, Lee L, Kim E, Hui T, Stoynov N, Nassar R, Moksa M, Cameron DM, Hirst M, Gsponer J, Mayor T. (2017). The [PSI+] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI+] cells can promote aneuploidy. Sci Rep. 7, 8442 (view full text)

Alvaro J. Amor, Dominic T. Castanzo, Sean P. Delany, Daniel M. Selechnik, Alex van Ooy, Dale M. Cameron*. (2015). The ribosome-associated complex antagonizes prion formation in yeast. Prion 9, 144-64 (view full text)
(Undergraduate student collaborators are bolded)   * Corresponding author

Henry TC, Power JE, Kerwin CL, Mohammed A, Weissman JS, Cameron D, Wykoff D. (2011). Systematic screen of Schizosaccharomyces pombe deletion collection uncovers parallel evolution of the phosphate signal transduction pathway in yeasts. Eukaryotic Cell 10, 198-206

Gregory, S.T., Demirci, H., Carr, J.F., Belardinelli, R., Thompson, J.R.,Cameron, D.M., Rodriguez-Correa, D., Murphy, F., Jogl, G. & Dahlberg, A.E. (2010). Genetic and crystallographic approaches to investigating ribosome structure and function. In M. Rodnina, W. Wintermeyer & R. Green (Eds.), Ribosomes: Structure, Function and Dynamics. Vienna, New York: Springer-Verlag.

Breslow DK§, Cameron DM§, Collins SR, Schuldiner M, Stewart-Ornstein J, Newman HW, Braun S, Madhani HD, Krogan NJ, Weissman JS. (2008). A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nature Methods 5, 711-718.
§co-first authors
(Featured as a Research Highlight in Nature Reviews Genetics 9, 571)