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J. Biol. Chem., Vol. 278, Issue 32, 30199-30205, August 8, 2003
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From the
Laboratoire d'Enzymologie et Biochimie
Structurales, CNRS, 91198 Gif-sur-Yvette Cedex, France,
Chemical Resources Laboratory, Tokyo Institute
of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan, and
¶PRESTO, Japan Science and Technology
Corporation, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan
The [URE3] phenotype in Saccharomyces cerevisiae propagates by a
prion mechanism, involving the aggregation of the normally soluble and highly
helical protein Ure2. Previous data have shown that the protein spontaneously
forms in vitro long, straight, insoluble fibrils at neutral pH that
are similar to amyloids in that they bind Congo red and show green-yellow
birefringence and have an increased resistance to proteolysis. These fibrils
are not amyloids as they are devoid of a cross-
core. Here we further
document the mechanism of assembly of Ure2p into fibrils. The critical
concentration for Ure2p assembly is measured, and the minimal size of the
nuclei that are the precursors of Ure2p fibrils is determined. Our data
indicate that the assembly process is irreversible. As a consequence, the
critical concentration is very low. By analyzing the elongation rates of
preformed fibrils and combining the results with single-fiber imaging
experiments of a variant Ure2p labeled by fluorescent dyes, we reveal the
polarity of the fibrils and differences in the elongation rates at their ends.
These results bring novel insight in the process of Ure2p assembly into
fibrils and the mechanism of propagation of yeast prions.
Received for publication, March 24, 2003 , and in revised form, May 19, 2003.
* This work was funded by the French Ministry of Research and Technology, the CNRS, the Association pour la Recherche sur le Cancer, and grants-in-aid for scientific research from the Japanese Ministry of Education, Science, Sports, and Culture. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
This work is dedicated to professor Claude Hélène.
|| To whom correspondence should be addressed. Tel.: 33-169823503; Fax: 33-169823129; E-mail: melki{at}lebs.cnrs-gif.fr.
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