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Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35–NM

Title data

Hess, Simone ; Lindquist, Susan L. ; Scheibel, Thomas:
Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35–NM.
In: EMBO Reports. Vol. 8 (1 December 2007) Issue 12 . - pp. 1196-1201.
ISSN 1469-3178
DOI: https://doi.org/10.1038/sj.embor.7401096

Official URL: Volltext

Abstract in another language

The self-perpetuating conformational change of the translation termination factor Sup35 is associated with a prion phenomenon of Saccharomyces cerevisiae. In vitro, the prion-determining region (NM) of Sup35 assembles into amyloid-like fibres through a mechanism of nucleated conformational conversion. Here, we describe an alternative assembly pathway of NM that produces filaments that are composed of b-strands and random coiled regions with several-fold smaller diameters than the amyloid fibres. NM filaments are not detectable with either thioflavin T or
Congo Red and do not show SDS or protease resistance. As
filaments do not self-convert into fibres and do not act as seed,they are not intermediates of amyloid fibre formation. Instead, they represent a stable off-pathway form. Similar to mammalian prion proteins, Sup35 contains oligopeptide repeats located in the NM region. We found that the number of repeats determines the partitioning of the protein between filaments and amyloid-like fibres. Low numbers of repeats favour the formation of the filamentous structure, whereas high numbers of repeats favour the formation of amyloid-like fibres.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: Der Artikel wurde zunächst online veröffentlicht am 02.11.2007
Keywords: filament; AFM; FTIR; oligopeptide repeats
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Faculties > Faculty of Engineering Science > Chair Biomaterials
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: No
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 17 Mar 2015 09:53
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/8399