| The yeast Sup35NM domain propagates as a prion in mammalian cells. | |
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MedLine Citation:
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PMID: 19114662 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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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:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-12-29 |
Journal Detail:
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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:
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Created Date: 2009-01-14 Completed Date: 2009-02-13 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 462-7 Citation Subset: IM |
Affiliation:
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Institute of Virology, Technische Universität München, Trogerstrasse 30, 81675 Munich, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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0/Peptide Termination Factors; 0/Prions; 0/SUP35 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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