bei Google ScholarTitelangaben
Jijun, Dong ; Bloom, Jesse ; Goncharov, Vladimir ; Chattopadhyay, Madhuri ; Millhauser, Glenn L. ; Lynn, David G. ; Scheibel, Thomas ; Lindquist, Susan L.:
Probing the Role of PrP Repeats in Conformational Conversion and Amyloid Assembly of Chimeric Yeast Prions.
In: The Journal of Biological Chemistry.
Bd. 282
(2007)
Heft 47
.
- S. 34204-34212.
ISSN 1083-351X
DOI: https://doi.org/10.1074/jbc.M704952200
Abstract
Oligopeptide repeats appear in many proteins that undergo conformational conversions to form amyloid, including the mammalian prion protein PrP and the yeast prion protein Sup35. Whereas the repeats in PrP have been studied more exhaustively, interpretation of these studies is confounded by the fact that many details of the PrP prion conformational conversion are not well understood. On the other hand, there is now a relatively good understanding of the factors that guide the conformational conversion of the Sup35 prion protein. To provide a general model for studying the role of oligopeptide repeats in prion conformational conversion and amyloid formation, we have substituted various numbers of the PrP octarepeats for the endogenous Sup35 repeats. The resulting chimeric proteins can adopt the [PSI+] prion state in yeast, and the stability of the prion state depends on the number of repeats. In vitro, these chimeric proteins form amyloid fibers, with more repeats leading to shorter lag phases and faster assembly rates. Both pH and the presence of metal ions modulate assembly kinetics of the chimeric proteins, and the extent of modulation is highly sensitive to the number of PrP repeats. This work offers new insight into the properties of the PrP octarepeats in amyloid assembly and prion formation. It also reveals new features of the yeast prion protein, and provides a level of control over yeast prion assembly that will be useful for future structural studies and for creating amyloid-based biomaterials.
Weitere Angaben
| 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 08:14 |
| Letzte Änderung: | 14 Feb 2023 12:21 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19525 |