NR AOCY
AU Balguerie,A.; Dos Reis,S.; Ritter,C.; Chaignepain,S.; Coulary-Salin,B.; Forge,V.; Bathany,K.; Lascu,I.; Schmitter,J.M.; Riek,R.; Saupe,S.J.
TI Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
QU EMBO Journal 2003 May 1; 22(9): 2071-81
IA http://www.pubmedcentral.gov/articlerender.fcgi?tool=pubmed&pubmedid=12727874
PT journal article
AB The [Het-s] infectious element of the fungus Podospora anserina is a prion protein involved in a genetically controlled cell death reaction termed heterokaryon incompatibility. Previous analyses indicate that [Het-s] propagates as a self-perpetuating amyloid aggregate. The HET-s protein is 289 amino acids in length. Herein, we identify the region of the HET-s protein that is responsible for amyloid formation and prion propagation. The region of HET-s spanning residues 218-289 forms amyloid fibers in vitro and allows prion propagation in vivo. Conversely, a C-terminal deletion in HET-s prevents amyloid aggregation in vitro and prion propagation in vivo, and abolishes the incompatibility function. In the soluble form of HET-s, the region from residue 1 to 227 forms a well-folded domain while the C-terminal region is highly flexible. Together, our data establish a domain structure-function relationship for HET-s amyloid formation, prion propagation and incompatibility activity.
MH Amino Acid Sequence; Circular Dichroism; Fungal Proteins/*chemistry/*physiology; Hydrolysis; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Recombinant Proteins/chemistry/metabolism; Sequence Homology, Amino Acid; Sordariales/*metabolism; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Support, Non-U.S. Gov't
AD Laboratoire de Genetique Moleculaire des Champignons, Service de Microscopie, UMR 5095 CNRS/Universite de Bordeaux 2, 1 rue Camille St Saens, 33077 Bordeaux cedex, France.
SP englisch
PO England