Document Detail


The yeast Sup35NM domain propagates as a prion in mammalian cells.
MedLine Citation:
PMID:  19114662     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Carmen Krammer; Dmitry Kryndushkin; Michael H Suhre; Elisabeth Kremmer; Andreas Hofmann; Alexander Pfeifer; Thomas Scheibel; Reed B Wickner; Hermann M Schätzl; Ina Vorberg
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-12-29
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  106     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2009-01-14     Completed Date:  2009-02-13     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  462-7     Citation Subset:  IM    
Affiliation:
Institute of Virology, Technische Universität München, Trogerstrasse 30, 81675 Munich, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Mice
Molecular Probe Techniques
Neuroblastoma / pathology*
Peptide Termination Factors
Prion Diseases / transmission*
Prions / adverse effects,  biosynthesis*
Saccharomyces cerevisiae Proteins / adverse effects*
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Peptide Termination Factors; 0/Prions; 0/SUP35 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins
Comments/Corrections

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