Structure and assembly properties of the yeast prion Ure2p.
The non-Mendelian phenotype [URE3] is due to a transmissible conformational change of the protein Ure2. The infectious protein form of Ure2p has lost its function and gained the capacity to transform the active form of the protein into an inactive form. The molecular basis of this conversion process is unknown. There are however indications that the conformational changes at the origin of the propagation of the inactive form of Ure2p in yeast cells are similar to those at the origin of the transition of PrPC into the scrapie-associated PrPSc form of the protein. To better understand the nature of the conformational changes at the origin of prion propagation, we have purified, characterized biochemically, examined the assembly properties and solved the crystal structure of Ure2p. Our data are presented below and a number of conclusions dealing with the molecular basis of the conversion of soluble Ure2p into its amyloid-forming state are derived.
Bousset
Luc
L
Laboratoire d'enzymologie et biochimie structurales, CNRS, Bât. 34, avenue de la terrasse, 91198 Gif-sur-Yvette, France.
Thual
Carine
C
Belrhali
Hassan
H
Morera
Solange
S
Melki
Ronald
R
D000682:Amyloid / Q000737:chemistry; D002942:Circular Dichroism; D003460:Crystallization; D019281:Dimerization; D005979:Glutathione Peroxidase; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D008958:Models, Molecular; D015394:Molecular Structure; D008970:Molecular Weight; D011328:Prions; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012995:Solubility
D000682:Amyloid; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae