The [URE3] Yeast Prion Results from Protein Aggregates That Differ from Amyloid Filaments Formed in Vitro

Ripaud, Leslie; Maillet, Laurent; Immel, Françoise; Durand, Fabien; Cullin, Christophe

doi:10.1074/jbc.m408792200

Cited by 12 publications

(12 citation statements)

References 39 publications

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“…4B) is roughly the same and is consistent with the profile previously obtained when ScUre2p was subjected to limited proteolysis under identical conditions to those used here (19,30,31). The main species observed is a 30-kDa species that corresponds to the functional domain of Ure2p (13,19). Overall, the different species generated upon PK treatment of either soluble or aggregated Sc or SpUre2p are populated in the same quantity under the same conditions for the two proteins.…”

Section: Volume 282 • Number 11 • March 16 2007supporting

confidence: 75%

“…It has been reported that extensive digestion of ScUre2p fibers with proteinase K leads to the production of a fuzzy band of low molecular weight corresponding to the prion domain (22). In our hands, we could not detect such a smear, even after adding additional proteinase K or incubating Sc or SpUre2p filaments for a longer period (13) (and data not shown). In an attempt to detect this prion domain, the proteinase K fragments were also examined by a Western blot analysis (Fig.…”

Section: Volume 282 • Number 11 • March 16 2007contrasting

confidence: 42%

“…The 6ϫ His tag was PCRamplified and inserted at the 3Ј-end of URE2 resulting in pET3a-URE2-His 6 (13). The full-length Ure2p Sp expression vector (pET-URE2 (Sp)-His 6 ) was obtained by amplifying by PCR a pUHE-URE2 (Sp) construct that encodes for Ure2p (Sp), using the following primers: 5Ј-CGGCATATGATGAATAAC-AACGGCAACC-3Ј and 5Ј -CCGCTCGAGTCATTCACCAC-GCAATGCC-3Ј.…”

Section: Methodsmentioning

confidence: 99%

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In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion

Immel¹,

Jiang

Wang

et al. 2007

Journal of Biological Chemistry

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The yeast Saccharomyces cerevisiae contains in its proteome at least three prion proteins. These proteins (Ure2p, Sup35p, and Rnq1p) share a set of remarkable properties. In vivo, they form aggregates that self-perpetuate their aggregation. This aggregation is controlled by Hsp104, which plays a major role in the growth and severing of these prions. In vitro, these prion proteins form amyloid fibrils spontaneously. is not well conserved in the hemiascomycetous yeasts and particularly in S. paradoxus. Here we demonstrated that the S. paradoxus Ure2p is able to form infectious amyloid. These fibrils are more resistant than S. cerevisiae Ure2p fibrils to shear force. The observation, in vivo, of a distinct aggregation pattern for GFP fusions confirms the higher propensity of SpUre2p to form fibrillar structures. Our in vitro and in vivo analysis of aggregation propensity of the S. paradoxus Ure2p provides an explanation for its loss of infective properties and suggests that this protein belongs to the non-prion amyloid world.The yeast prions represent an attractive and valuable model for understanding complex aspects of mammalian prion biology. The yeast system has provided the first experimental demonstration (1) of the "protein-only" concept proposed by J. Griffith (2) and developed by S. Prusiner (3) to explain the disconcerting biological properties of the infectious agent responsible for the transmissible spongiform encephalopathies.

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Section: Volume 282 • Number 11 • March 16 2007supporting

confidence: 75%

Section: Volume 282 • Number 11 • March 16 2007contrasting

confidence: 42%

Section: Methodsmentioning

confidence: 99%

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In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion

Immel¹,

Jiang

Wang

et al. 2007

Journal of Biological Chemistry

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“…Despite the above evidence, controversy over whether the prion form of Ure2 is amyloid remains (Bousset et al 2002b(Bousset et al , 2004Ripaud et al 2004;Fay et al 2005;Redeker et al 2007). A minority view is that the Ure2 globular domain is part of the fiber core because this domain is more ordered in in vitro Ure2 fibers made of full-length Ure2 vs. the PrD alone ).…”

Section: Models Of Prion Structuresmentioning

confidence: 99%

Prions in Yeast

2012

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The concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the "protein only" model of prion transmission was first proven using a yeast prion. Typically, known prions are ordered cross-b aggregates (amyloids). Recently, there has been an explosion in the number of recognized prions in yeast. Yeast continues to lead the way in understanding cellular control of prion propagation, prion structure, mechanisms of de novo prion formation, specificity of prion transmission, and the biological roles of prions. This review summarizes what has been learned from yeast prions.

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“…Upon entering the Wlamentous state, it undergoes a drastic conformational change as attested by its becoming highly resistant to proteases (Baxa et al, 2003;Ripaud et al, 2004;Taylor et al, 1999) and other lines of evidence Schlumpberger et al, 2000;Taylor et al, 1999). The predisposition for this conformational change seems to lie mainly in its amino acid composition, since Wve randomizations of the order of the amino acids of the N-domain sequence produced Ure2p variants that retained the ability to form Wlaments in vitro and become prions in vivo .…”

Section: Introductionmentioning

confidence: 95%