Literature DB >> 19519517

Hsp104 and prion propagation.

Nina V Romanova1, Yury O Chernoff.   

Abstract

High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular "disaggregase".

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Year:  2009        PMID： 19519517      PMCID： PMC2791106          DOI： 10.2174/092986609788490078

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


  78 in total

1.  Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  EMBO J       Date:  2002-01-15       Impact factor: 11.598

2.  Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.

Authors:  Anil G Cashikar; Eric C Schirmer; Douglas A Hattendorf; John R Glover; Melarkode S Ramakrishnan; Danielle M Ware; Susan L Lindquist
Journal:  Mol Cell       Date:  2002-04       Impact factor: 17.970

3.  The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation.

Authors:  P C Ferreira; F Ness; S R Edwards; B S Cox; M F Tuite
Journal:  Mol Microbiol       Date:  2001-06       Impact factor: 3.501

4.  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

5.  Initial process of polyglutamine aggregate formation in vivo.

Authors:  Y Kimura; S Koitabashi; A Kakizuka; T Fujita
Journal:  Genes Cells       Date:  2001-10       Impact factor: 1.891

6.  Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'.

Authors:  A S Borchsenius; R D Wegrzyn; G P Newnam; S G Inge-Vechtomov; Y O Chernoff
Journal:  EMBO J       Date:  2001-12-03       Impact factor: 11.598

7.  Nuclear aggregation of huntingtin is not prevented by deletion of chaperone Hsp104.

Authors:  F Cao; J J Levine; S H Li; X J Li
Journal:  Biochim Biophys Acta       Date:  2001-09-28

8.  Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.

Authors:  Giman Jung; Gary Jones; Daniel C Masison
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-08       Impact factor: 11.205

9.  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

10.  Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.

Authors:  Anatoli B Meriin; Xiaoqian Zhang; Xiangwei He; Gary P Newnam; Yury O Chernoff; Michael Y Sherman
Journal:  J Cell Biol       Date:  2002-06-10       Impact factor: 10.539
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  39 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.  Heat, pH induced aggregation and surface hydrophobicity of S. cerevesiae Ssa1 protein.

Authors:  Yusuf Tutar; Derya Arslan; Lütfi Tutar
Journal:  Protein J       Date:  2010-10       Impact factor: 2.371

Review 3.  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

Review 4.  Prions in yeast.

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

5.  The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.

Authors:  Kiran Aslam; Chai-Jui Tsai; Tony R Hazbun
Journal:  Prion       Date:  2016-11       Impact factor: 3.931

6.  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

7.  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

Review 8.  Epigenetic inheritance, prions and evolution.

Authors:  Johannes Manjrekar
Journal:  J Genet       Date:  2017-07       Impact factor: 1.166

9.  Exploring prion protein biology in flies: genetics and beyond.

Authors:  Diego E Rincon-Limas; Sergio Casas-Tinto; Pedro Fernandez-Funez
Journal:  Prion       Date:  2010-01-30       Impact factor: 3.931

10.  Regulation of chaperone effects on a yeast prion by cochaperone Sgt2.

Authors:  Denis A Kiktev; Jesse C Patterson; Susanne Müller; Bhawana Bariar; Tao Pan; Yury O Chernoff
Journal:  Mol Cell Biol       Date:  2012-10-08       Impact factor: 4.272
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