Literature DB >> 21717344

Fungal prions: structure, function and propagation.

Mick F Tuite1, Ricardo Marchante, Vitaly Kushnirov.   

Abstract

Prions are not uniquely associated with rare fatal neurodegenerative diseases in the animal kingdom; prions are also found in fungi and in particular the yeast Saccharomyces cerevisiae. As with animal prions, fungal prions are proteins able to exist in one or more self-propagating alternative conformations, but show little primary sequence relationship with the mammalian prion protein PrP. Rather, fungal prions represent a relatively diverse collection of proteins that participate in key cellular processes such as transcription and translation. Upon switching to their prion form, these proteins can generate stable, sometimes beneficial, changes in the host cell phenotype. Much has already been learnt about prion structure, and propagation and de novo generation of the prion state through studies in yeast and these findings are reviewed here.

Entities:  

Mesh:

Substances:

Year:  2011        PMID: 21717344     DOI: 10.1007/128_2011_172

Source DB:  PubMed          Journal:  Top Curr Chem        ISSN: 0340-1022


  14 in total

Review 1.  Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.

Authors:  Jens Tyedmers
Journal:  Prion       Date:  2012-07-01       Impact factor: 3.931

Review 2.  Protein rescue from aggregates by powerful molecular chaperone machines.

Authors:  Shannon M Doyle; Olivier Genest; Sue Wickner
Journal:  Nat Rev Mol Cell Biol       Date:  2013-10       Impact factor: 94.444

3.  The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β.

Authors:  Ulrike K Resenberger; Veronika Müller; Lisa M Munter; Michael Baier; Gerd Multhaup; Mark R Wilson; Konstanze F Winklhofer; Jörg Tatzelt
Journal:  J Biol Chem       Date:  2012-10-31       Impact factor: 5.157

4.  The effects of glutamine/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains.

Authors:  Jenifer E Shattuck; Aubrey C Waechter; Eric D Ross
Journal:  Prion       Date:  2017-06-30       Impact factor: 3.931

5.  S. pombe placed on the prion map.

Authors:  Jacqueline Hayles
Journal:  Microb Cell       Date:  2017-02-03

6.  Exploring the basis of [PIN(+)] variant differences in [PSI(+)] induction.

Authors:  Jaya Sharma; Susan W Liebman
Journal:  J Mol Biol       Date:  2013-06-14       Impact factor: 5.469

7.  Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.

Authors:  Helen R Saibil; Anja Seybert; Anja Habermann; Juliane Winkler; Mikhail Eltsov; Mario Perkovic; Daniel Castaño-Diez; Margot P Scheffer; Uta Haselmann; Petr Chlanda; Susan Lindquist; Jens Tyedmers; Achilleas S Frangakis
Journal:  Proc Natl Acad Sci U S A       Date:  2012-08-27       Impact factor: 11.205

Review 8.  Microbial manipulation of the amyloid fold.

Authors:  William H DePas; Matthew R Chapman
Journal:  Res Microbiol       Date:  2012-10-27       Impact factor: 3.992

9.  Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants.

Authors:  Jennifer E Dulle; Heather L True
Journal:  Prion       Date:  2013-09-24       Impact factor: 3.931

10.  Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus.

Authors:  Kendra K Frederick; Vladimir K Michaelis; Björn Corzilius; Ta-Chung Ong; Angela C Jacavone; Robert G Griffin; Susan Lindquist
Journal:  Cell       Date:  2015-10-08       Impact factor: 41.582

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.