NR ADXZ
AU Fernandez-Bellot,E.; Cullin,C.
TI The protein-only theory and the yeast Saccharomyces cerevisiae: the prions and the propagons.
QU Cellular and Molecular Life Science 2001 Nov; 58(12-13): 1857-78
PT journal article; review; review, tutorial
AB The yeast prions represent a very attractive and tractable model for investigating the prion world. The more extensively studied yeast prion [PSI] leads to a propagation model that links auto-aggregation in amyloid formation and inactivation of the cellular function of the yeast 'prion protein' Sup35p. The other prion model, [URE3], appears to be similar in some genetic and biochemical properties. The characterisation of both Sup35p and Ure2p, the two 'prion proteins', mainly focusing on their aggregation properties, support this model. However, some important differences still exist that should be examined carefully. In particular, we have shown that Ure2p aggregation in vivo (monitored by fluorescence of Ure2-GFP fusion) does not necessarily give rise to a [URE3] phenotype. Comparisons of these two systems as well as more recent experiments are discussed in this review.
ZR 84
MH Animal; Fungal Proteins/chemistry/genetics/*metabolism; Heat-Shock Proteins/metabolism; Heat-Shock Proteins 70/metabolism; Luminescent Proteins/genetics/metabolism; Models, Biological; Phenotype; Prions/chemistry/genetics/*metabolism; Recombinant Fusion Proteins/genetics/metabolism; Saccharomyces cerevisiae/genetics/*physiology; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism
AD Institut de Biochimie et Genetique Cellulaires, Bordeaux, France.
SP englisch
PO Schweiz