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Krammer, Carmen ; Suhre, Michael H. ; Kremmer, Elisabeth ; Diemer, Claudia ; Hess, Simone ; Schätzl, Hermann M. ; Scheibel, Thomas ; Vorberg, Ina M.:
Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells.
In: The FASEB Journal.
Bd. 22
(2008)
Heft 3
.
- S. 762-773.
ISSN 0892-6638
DOI: https://doi.org/10.1096/fj.07-8733com
Abstract
In mammalian prion diseases, an abnormally folded, aggregated form of the prion protein (PrPSc) appears to catalyze a conformational switch of its cellular isoform (PrPC) to an aggregated state. A similar prion-like phenomenon has been reported for the Saccharomyces cerevisiae translation termination factor Sup35p that can adopt a self-propagating conformation. We have compared aggregation propensities of chimeric proteins derived from the Sup35p prion domain NM and PrP in vitro and in the cytosol of mammalian cells. Sup35p-NM and PrP displayed strikingly different aggregation behaviors when expressed in mammalian cells, with NM remaining soluble and cytosolic PrP spontaneously aggregating due to the globular domain of PrP. When fused to PrP90–230, Sup35p-M exhibited an inhibitory effect for nucleation but increased aggregate growth, potentially by facilitating recruitment of newly synthesized chimeric proteins into the growing aggregates. This effect, however, could, to some extent, be counteracted by the prion-forming region Sup35p-N, thereby increasing aggregate frequency. Interestingly, a lowered nucleation rate was also observed in the presence of the amino-terminal region of PrP, suggesting that Sup35p-M and PrP23–90 share some biological function in prion protein assembly. Our results provide new insights into prion protein aggregation behaviors, demonstrating the impact of dynamic interactions between prion domains and suggesting that aggregation of yeast and mammalian prion proteins is strongly influenced by yet unidentified cellular conditions or factors.—Krammer C., Suhre, M. H., Kremmer, E., Diemer, C., Hess, S., Schätzl, H. M., Scheibel, T., Vorberg, I. Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells
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| Publikationsform: | Artikel in einer Zeitschrift |
|---|---|
| Begutachteter Beitrag: | Ja |
| Institutionen der Universität: | Fakultäten Fakultäten > Fakultät für Ingenieurwissenschaften Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel Profilfelder > Advanced Fields > Neue Materialien Profilfelder > Advanced Fields > Molekulare Biowissenschaften Profilfelder > Advanced Fields > Polymer- und Kolloidforschung Profilfelder > Emerging Fields > Lebensmittel- und Gesundheitswissenschaften Profilfelder Profilfelder > Advanced Fields Profilfelder > Emerging Fields |
| Titel an der UBT entstanden: | Ja |
| Themengebiete aus DDC: | 600 Technik, Medizin, angewandte Wissenschaften 600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften |
| Eingestellt am: | 24 Sep 2015 07:29 |
| Letzte Änderung: | 26 Nov 2015 10:51 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19523 |