Literature DB >> 12142498

Prions as protein-based genetic elements.

Susan M Uptain1, Susan Lindquist.   

Abstract

Fungal prions are fascinating protein-based genetic elements. They alter cellular phenotypes through self-perpetuating changes in protein conformation and are cytoplasmically partitioned from mother cell to daughter. The four prions of Saccharomyces cerevisiae and Podospora anserina affect diverse biological processes: translational termination, nitrogen regulation, inducibility of other prions, and heterokaryon incompatibility. They share many attributes, including unusual genetic behaviors, that establish criteria to identify new prions. Indeed, other fungal traits that baffled microbiologists meet some of these criteria and might be caused by prions. Recent research has provided notable insight about how prions are induced and propagated and their many biological roles. The ability to become a prion appears to be evolutionarily conserved in two cases. [PSI(+)] provides a mechanism for genetic variation and phenotypic diversity in response to changing environments. All available evidence suggests that prions epigenetically modulate a wide variety of fundamental biological processes, and many await discovery.

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Year:  2002        PMID: 12142498     DOI: 10.1146/annurev.micro.56.013002.100603

Source DB:  PubMed          Journal:  Annu Rev Microbiol        ISSN: 0066-4227            Impact factor:   15.500


  90 in total

Review 1.  The unfolded protein response in protein aggregating diseases.

Authors:  Alexander Gow; Ramaswamy Sharma
Journal:  Neuromolecular Med       Date:  2003       Impact factor: 3.843

2.  Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.

Authors:  Michael E Bradley; Susan W Liebman
Journal:  Genetics       Date:  2003-12       Impact factor: 4.562

3.  Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation.

Authors:  Erwann Rousseau; Benjamin Dehay; Léa Ben-Haïem; Yvon Trottier; Michel Morange; Anne Bertolotti
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-21       Impact factor: 11.205

4.  Sonication of proteins causes formation of aggregates that resemble amyloid.

Authors:  Peter B Stathopulos; Guenter A Scholz; Young-Mi Hwang; Jessica A O Rumfeldt; James R Lepock; Elizabeth M Meiering
Journal:  Protein Sci       Date:  2004-09-30       Impact factor: 6.725

5.  Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function.

Authors:  Zhiqiang Du; Emily T Crow; Hyun Seok Kang; Liming Li
Journal:  Mol Cell Biol       Date:  2010-08-02       Impact factor: 4.272

6.  Generation of prions in vitro and the protein-only hypothesis.

Authors:  Rodrigo Diaz-Espinoza; Claudio Soto
Journal:  Prion       Date:  2010-04-05       Impact factor: 3.931

Review 7.  More than Just a Phase: Prions at the Crossroads of Epigenetic Inheritance and Evolutionary Change.

Authors:  Anupam K Chakravarty; Daniel F Jarosz
Journal:  J Mol Biol       Date:  2018-07-19       Impact factor: 5.469

Review 8.  Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.

Authors:  Julie A Moreno; Glenn C Telling
Journal:  Methods Mol Biol       Date:  2017

Review 9.  Prion diseases and their biochemical mechanisms.

Authors:  Nathan J Cobb; Witold K Surewicz
Journal:  Biochemistry       Date:  2009-03-31       Impact factor: 3.162

10.  Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers.

Authors:  Sarah Hanna-Addams; Zhigao Wang
Journal:  J Vis Exp       Date:  2018-04-26       Impact factor: 1.355

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