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Krammer, C.* ; Kryndushkin, D.* ; Suhre, M.H.* ; Kremmer, E. ; Hofmann, A.* ; Pfeifer, A.* ; Scheibel, T.* ; Wickner, R.B.* ; Schatzl, H.M.* ; Vorberg, I.*

The yeast Sup35NM domain propagates as a prion in mammalian cells.

Proc. Natl. Acad. Sci. U.S.A. 106, 462-467 (2009)
DOI PMC
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Prions are infectious, self-propagating amyloid-like protein aggregates of mammals and fungi. We have studied aggregation propensities of a yeast prion domain in cell culture to gain insights into general mechanisms of prion replication in mammalian cells. Here, we report the artificial transmission of a yeast prion across a phylogenetic kingdom. HA epitope-tagged yeast Sup35p prion domain NM was stably expressed in murine neuroblastoma cells. Although cytosolically expressed NM-HA remained soluble, addition of fibrils of bacterially produced Sup35NM to the medium efficiently induced appearance of phenotypically and biochemically distinct NM- HA aggregates that were inherited by daughter cells. Importantly, NM-HA aggregates also were infectious to recipient mammalian cells expressing soluble NM-HA and, to a lesser extent, to yeast. The fact that the yeast Sup35NM domain can propagate as a prion in neuroblastoma cells strongly argues that cellular mechanisms support prion-like inheritance in the mammalian cytosol.
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Publication type Article: Journal article
Document type Scientific Article
Keywords PrP; Sup35; saccharomyces-cerevisiae; het-s; psi+ prion; in-vitro; protein; determinant; strains; psi(+); chaperones; hsp104
Language english
Publication Year 2009
HGF-reported in Year 2009
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Quellenangaben Volume: 106, Issue: 2, Pages: 462-467 Article Number: , Supplement: ,
Publisher National Academy of Sciences
Reviewing status Peer reviewed
PSP Element(s) G-501700-003
PubMed ID 19114662
Scopus ID 58849091748
Erfassungsdatum 2009-07-09