Literature DB >> 19519522

Application of GFP-labeling to study prions in yeast.

Lois E Greene1, Yang-Nim Park, Daniel C Masison, Evan Eisenberg.   

Abstract

Fluorescent live cell imaging has recently been used in numerous studies to examine prions in yeast. These fluorescence studies take advantage of the fact that unlike the normally folded form, the misfolded amyloid form of the prion protein is aggregated. The studies have used fluorescence to identify new prions, to study the transmission of prion from mother to daughter, and to understand the role of molecular chaperones in this transmission. The use of fluorescence imaging complements the more standard methods used to study prion propagation. This review discusses the various studies that have taken advantage of fluorescence imaging technique particularly in regard to understanding the transmission and curing of the [PSI(+)], the prion form of the translation termination factor Sup35p.

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Year:  2009        PMID: 19519522      PMCID: PMC2696060          DOI: 10.2174/092986609788490221

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  38 in total

1.  The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)].

Authors:  P Zhou; I L Derkatch; S W Liebman
Journal:  Mol Microbiol       Date:  2001-01       Impact factor: 3.501

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.  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

4.  A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion.

Authors:  A H DePace; A Santoso; P Hillner; J S Weissman
Journal:  Cell       Date:  1998-06-26       Impact factor: 41.582

Review 5.  Prions of yeast and fungi. Proteins as genetic material.

Authors:  R B Wickner; H K Edskes; M L Maddelein; K L Taylor; H Moriyama
Journal:  J Biol Chem       Date:  1999-01-08       Impact factor: 5.157

Review 6.  Prion protein biology.

Authors:  S B Prusiner; M R Scott; S J DeArmond; F E Cohen
Journal:  Cell       Date:  1998-05-01       Impact factor: 41.582

7.  Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae.

Authors:  S S Eaglestone; L W Ruddock; B S Cox; M F Tuite
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-04       Impact factor: 11.205

8.  Mechanism of prion loss after Hsp104 inactivation in yeast.

Authors:  R D Wegrzyn; K Bapat; G P Newnam; A D Zink; Y O Chernoff
Journal:  Mol Cell Biol       Date:  2001-07       Impact factor: 4.272

9.  Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions.

Authors:  G Jung; D C Masison
Journal:  Curr Microbiol       Date:  2001-07       Impact factor: 2.188

10.  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

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  10 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

2.  Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.

Authors:  Yang-Nim Park; Xiaohong Zhao; Yang-In Yim; Horia Todor; Robyn Ellerbrock; Michael Reidy; Evan Eisenberg; Daniel C Masison; Lois E Greene
Journal:  Eukaryot Cell       Date:  2014-03-14

3.  Curing of [PSI+] by Hsp104 Overexpression: Clues to solving the puzzle.

Authors:  Lois E Greene; Xiaohong Zhao; Evan Eisenberg
Journal:  Prion       Date:  2018-02-02       Impact factor: 3.931

4.  Septin-containing barriers control the differential inheritance of cytoplasmic elements.

Authors:  Alan Michael Tartakoff; Ilya Aylyarov; Purnima Jaiswal
Journal:  Cell Rep       Date:  2012-12-27       Impact factor: 9.423

5.  Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.

Authors:  Xiaohong Zhao; Ramon Rodriguez; Rebecca E Silberman; Joseph M Ahearn; Sheela Saidha; Kaelyn C Cummins; Evan Eisenberg; Lois E Greene
Journal:  J Biol Chem       Date:  2017-04-03       Impact factor: 5.157

6.  Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation.

Authors:  Yang-Nim Park; David Morales; Emily H Rubinson; Daniel Masison; Evan Eisenberg; Lois E Greene
Journal:  PLoS One       Date:  2012-06-18       Impact factor: 3.240

7.  Osmolytes ameliorate the effects of stress in the absence of the heat shock protein Hsp104 in Saccharomyces cerevisiae.

Authors:  Arnab Bandyopadhyay; Indrani Bose; Krishnananda Chattopadhyay
Journal:  PLoS One       Date:  2019-09-19       Impact factor: 3.240

Review 8.  Mechanisms for Curing Yeast Prions.

Authors:  Lois E Greene; Farrin Saba; Rebecca E Silberman; Xiaohong Zhao
Journal:  Int J Mol Sci       Date:  2020-09-07       Impact factor: 5.923

Review 9.  Biochemical Principles in Prion-Based Inheritance.

Authors:  Emily M Dennis; David M Garcia
Journal:  Epigenomes       Date:  2022-01-25

10.  Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.

Authors:  Chan-Gi Pack; Yuji Inoue; Takashi Higurashi; Shigeko Kawai-Noma; Daigo Hayashi; Elizabeth Craig; Hideki Taguchi
Journal:  BMB Rep       Date:  2017-09       Impact factor: 4.778

  10 in total

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