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Literature DB >> 17392510

Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.

Abstract

The [URE3] and [PSI(+)] prions are infectious amyloid forms of Ure2p and Sup35p. Several chaperones influence prion propagation: Hsp104p overproduction destabilizes [PSI(+)], whereas [URE3] is sensitive to excess of Ssa1p or Ydj1p. Here, we show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3]. Sse1p and Fes1p are nucleotide exchange factors for Ssa1p. Interestingly, deletion of either SSE1 or FES1 completely blocked [URE3] propagation. In addition, deletion of SSE1 also interfered with [PSI(+)] propagation.

Entities: Chemical Gene Species

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Year: 2007 PMID： 17392510 PMCID： PMC1877104 DOI： 10.1091/mbc.e07-02-0128

Source DB: PubMed Journal: Mol Biol Cell ISSN： 1059-1524 Impact factor: 4.138

36 in total

1. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

Authors: G P Newnam; R D Wegrzyn; S L Lindquist; Y O Chernoff
Journal: Mol Cell Biol Date: 1999-02 Impact factor: 4.272

2. 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

3. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.

Authors: Christine Schwimmer; Daniel C Masison
Journal: Mol Cell Biol Date: 2002-06 Impact factor: 4.272

4. Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.

Authors: Dmitry S Kryndushkin; Vladimir N Smirnov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
Journal: J Biol Chem Date: 2002-03-28 Impact factor: 5.157

5. Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding.

Authors: Gary Jones; Youtao Song; Seyung Chung; Daniel C Masison
Journal: Mol Cell Biol Date: 2004-05 Impact factor: 4.272

6. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.

Authors: Dmitry S Kryndushkin; Ilya M Alexandrov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
Journal: J Biol Chem Date: 2003-09-24 Impact factor: 5.157

7. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast.

Authors: B Tibor Roberts; Hiromitsu Moriyama; Reed B Wickner
Journal: Yeast Date: 2004-01-30 Impact factor: 3.239

8. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast.

Authors: F Lacroute
Journal: J Bacteriol Date: 1971-05 Impact factor: 3.490

9. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.

Authors: Jennifer L Goeckeler; Andi Stephens; Paul Lee; Avrom J Caplan; Jeffrey L Brodsky
Journal: Mol Biol Cell Date: 2002-08 Impact factor: 4.138

10. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.

Authors: Lance Shaner; Amy Trott; Jennifer L Goeckeler; Jeffrey L Brodsky; Kevin A Morano
Journal: J Biol Chem Date: 2004-03-17 Impact factor: 5.157

64 in total

1. Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity.

Authors: Xinping Xu; Evans Boateng Sarbeng; Christina Vorvis; Divya Prasanna Kumar; Lei Zhou; Qinglian Liu
Journal: J Biol Chem Date: 2011-12-08 Impact factor: 5.157

Review 2. Modulation and elimination of yeast prions by protein chaperones and co-chaperones.

Authors: Michael Reidy; Daniel C Masison
Journal: Prion Date: 2011-10-01 Impact factor: 3.931

3. The yeast Sup35NM domain propagates as a prion in mammalian cells.

Authors: Carmen Krammer; Dmitry Kryndushkin; Michael H Suhre; Elisabeth Kremmer; Andreas Hofmann; Alexander Pfeifer; Thomas Scheibel; Reed B Wickner; Hermann M Schätzl; Ina Vorberg
Journal: Proc Natl Acad Sci U S A Date: 2008-12-29 Impact factor: 11.205

Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.

1. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

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

3. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.

4. Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.

5. Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding.

6. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.

7. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast.

8. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast.

9. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.

10. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.

1. Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity.

Review 2. Modulation and elimination of yeast prions by protein chaperones and co-chaperones.

3. The yeast Sup35NM domain propagates as a prion in mammalian cells.

4. The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity.

Review 5. Influence of Hsp70s and their regulators on yeast prion propagation.

6. Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.

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

8. The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype.

9. Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion.

Review 10. A brief overview of the Swi1 prion-[SWI+].