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Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.
Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, Forge V, Bathany K, Lascu I, Schmitter JM, Riek R, Saupe SJ.
Laboratoire de Genetique Moleculaire des Champignons, Service de Microscopie and Laboratoire d'Enzymologie Moleculaire, Institut de Biochimie et de Genetique Cellulaires, UMR 5095 CNRS/Universite de Bordeaux 2, 1 rue Camille St Saens, 33077 Bordeaux cedex, Institut Europeen de Chimie et Biologie, CNRS FRE 2247, 16 Av. Pey Berland, 33607 Pessac cedex, Laboratoire de Biophysique Moleculaire et Cellulaire, UMR 5090, Departement de Biologie Moleculaire et Structurale, CEA-Grenoble, 17 rue de Martyrs, 38054 Grenoble cedex 9, France and Structural Biology Laboratory, The Salk Institute for Biological Studies, PO Box 85800, San Diego, CA 92186-5800, USA Corresponding author e-mail: sven.saupe@ibgc.u-bordeaux2.frA.Balguerie and S.Dos Reis contributed equally to this work
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.
PMID: 12727874 [PubMed - as supplied by publisher]
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