Literature DB >> 20484678

Conversion of a yeast prion protein to an infectious form in bacteria.

Sean J Garrity1, Viknesh Sivanathan, Jijun Dong, Susan Lindquist, Ann Hochschild.   

Abstract

Prions are infectious, self-propagating protein aggregates that have been identified in evolutionarily divergent members of the eukaryotic domain of life. Nevertheless, it is not yet known whether prokaryotes can support the formation of prion aggregates. Here we demonstrate that the yeast prion protein Sup35 can access an infectious conformation in Escherichia coli cells and that formation of this material is greatly stimulated by the presence of a transplanted [PSI(+)] inducibility factor, a distinct prion that is required for Sup35 to undergo spontaneous conversion to the prion form in yeast. Our results establish that the bacterial cytoplasm can support the formation of infectious prion aggregates, providing a heterologous system in which to study prion biology.

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Year:  2010        PMID: 20484678      PMCID: PMC2890818          DOI: 10.1073/pnas.0913280107

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  45 in total

1.  Creating a protein-based element of inheritance.

Authors:  L Li; S Lindquist
Journal:  Science       Date:  2000-01-28       Impact factor: 47.728

2.  Rnq1: an epigenetic modifier of protein function in yeast.

Authors:  N Sondheimer; S Lindquist
Journal:  Mol Cell       Date:  2000-01       Impact factor: 17.970

3.  Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein.

Authors:  H E Sparrer; A Santoso; F C Szoka; J S Weissman
Journal:  Science       Date:  2000-07-28       Impact factor: 47.728

4.  Prions affect the appearance of other prions: the story of [PIN(+)].

Authors:  I L Derkatch; M E Bradley; J Y Hong; S W Liebman
Journal:  Cell       Date:  2001-07-27       Impact factor: 41.582

Review 5.  Prions as protein-based genetic elements.

Authors:  Susan M Uptain; Susan Lindquist
Journal:  Annu Rev Microbiol       Date:  2002-01-30       Impact factor: 15.500

6.  Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion.

Authors:  L Z Osherovich; J S Weissman
Journal:  Cell       Date:  2001-07-27       Impact factor: 41.582

7.  A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen.

Authors:  Julie Nemecek; Toru Nakayashiki; Reed B Wickner
Journal:  Proc Natl Acad Sci U S A       Date:  2009-01-27       Impact factor: 11.205

8.  Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast.

Authors:  Frédérique Ness; Paulo Ferreira; Brian S Cox; Mick F Tuite
Journal:  Mol Cell Biol       Date:  2002-08       Impact factor: 4.272

9.  Analysis of yeast prion aggregates with amyloid-staining compound in vivo.

Authors:  Yoko Kimura; Sumiko Koitabashi; Takashi Fujita
Journal:  Cell Struct Funct       Date:  2003-06       Impact factor: 2.212

10.  A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

Authors:  Simon Alberti; Randal Halfmann; Oliver King; Atul Kapila; Susan Lindquist
Journal:  Cell       Date:  2009-04-03       Impact factor: 41.582

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  28 in total

Review 1.  Modeling human neurodegenerative diseases in transgenic systems.

Authors:  Miguel A Gama Sosa; Rita De Gasperi; Gregory A Elder
Journal:  Hum Genet       Date:  2011-12-14       Impact factor: 4.132

2.  A bacterial global regulator forms a prion.

Authors:  Andy H Yuan; Ann Hochschild
Journal:  Science       Date:  2017-01-13       Impact factor: 47.728

3.  Mammalian prion amyloid formation in bacteria.

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Journal:  Prion       Date:  2016-03-03       Impact factor: 3.931

Review 4.  Prions in yeast.

Authors:  Susan W Liebman; Yury O Chernoff
Journal:  Genetics       Date:  2012-08       Impact factor: 4.562

5.  Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.

Authors:  Morgan E DeSantis; Eunice H Leung; Elizabeth A Sweeny; Meredith E Jackrel; Mimi Cushman-Nick; Alexandra Neuhaus-Follini; Shilpa Vashist; Matthew A Sochor; M Noelle Knight; James Shorter
Journal:  Cell       Date:  2012-11-09       Impact factor: 41.582

6.  Aggregation interplay between variants of the RepA-WH1 prionoid in Escherichia coli.

Authors:  Laura Molina-García; Rafael Giraldo
Journal:  J Bacteriol       Date:  2014-05-02       Impact factor: 3.490

7.  Generating extracellular amyloid aggregates using E. coli cells.

Authors:  Viknesh Sivanathan; Ann Hochschild
Journal:  Genes Dev       Date:  2012-11-19       Impact factor: 11.361

8.  RepA-WH1 prionoid: a synthetic amyloid proteinopathy in a minimalist host.

Authors:  Rafael Giraldo; Susana Moreno-Díaz de la Espina; M Elena Fernández-Tresguerres; Fátima Gasset-Rosa
Journal:  Prion       Date:  2011-04-01       Impact factor: 3.931

Review 9.  Physiological and environmental control of yeast prions.

Authors:  Tatiana A Chernova; Keith D Wilkinson; Yury O Chernoff
Journal:  FEMS Microbiol Rev       Date:  2013-12-04       Impact factor: 16.408

10.  Biofilm inhibitors that target amyloid proteins.

Authors:  Diego Romero; Edgardo Sanabria-Valentín; Hera Vlamakis; Roberto Kolter
Journal:  Chem Biol       Date:  2013-01-24
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