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The yeast Sup35NM domain propagates as a prion in mammalian cells.
Proc. Natl. Acad. Sci. U.S.A. 106, 462-467 (2009)
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
PrP; Sup35; saccharomyces-cerevisiae; het-s; psi+ prion; in-vitro; protein; determinant; strains; psi(+); chaperones; hsp104
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Band: 106,
Heft: 2,
Seiten: 462-467
Verlag
National Academy of Sciences
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Molecular Immunology (IMI)