Papers for Journal Club

Wickner, R.B. (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569

The seminal paper that established the phenomenological link between mammalian prions and mysterious epigenetic phenomena of yeast.

Chernoff, Y.O., et al. (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [PSI+]. Science 268, 880-884

The discovery that prions in yeast propagate with the assistance of host factors, namely Hsp104, that are necessary for protein disaggregation.

Serio, T.R., et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317-1321

One of the first examinations of amyloid formation by a prion determinant, suggesting amyloid polymerization as the mechanism for prion propagation.

Si, K., et al. (2003) A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 115, 879-891

The paper uses yeast as a tool to characterize the prion forming potential of an exogenous protein involved in learning and memory. This paper greatly broadens the “prion” umbrella to include a physiological process involving a long-term molecular switch.

True, H.L., et al. (2004) Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431, 184-187

An investigation of the types of phenotypes revealed by [PSI+], their complexity, and possible implications for the evolution of yeast.

Tanaka, M., et al. (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585-589

A mathematical treatise that explains how conformational characteristics of the amyloid fiber translate to differences in elongation rates and severing rates that in turn determine a prion strain’s strength and stability.

Alberti, S., et al. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137, 146-158

A recent approach to address the broad question of prion prevalence in a representative simple eukaryote. Highlights the amyloid-like character of prions and their relationship with molecular chaperones, and uses the modular nature of prion domains to discover new prion proteins.

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