10 Citations (Scopus)

Abstract

Endogenous yeast amyloids that control heritable traits and are frequently used as models for human amyloid diseases are termed yeast prions. Yeast prions, including the best studied ones ([PSI+] and [URE3]), propagate via intimate interactions with molecular chaperones. Different yeast prions exhibit differential responses to changes in levels, functionality or localization of the components of chaperone machinery. Here, we provide additional data confirming differential effects of chaperones (and specifically, Hsp40s) on yeast prions and summarize current knowledge of the mechanisms underlying chaperone specificities. Contrary to frequent statements in literature, overproduction of the Hsp104 chaperone antagonizes both [PSI+] and [URE3] prions, while overproduction of the Hsp70-Ssa1 chaperone antagonizes [URE3] prion only in some, but not in all strains. Recently, we demonstrated that the relocalization of a fraction of the Hsp40 chaperone Sis1 from the cytosol to the nucleus by the chaperone-sorting factor Cur1 exhibits opposite effects on [PSI+] and [URE3] prions. We suggest that the response of prions to changes in Sis1 localization represents a combination of the effects of Sis1 shortage on fragmentation of prion aggregates and on malpartition of prion aggregates during a cell division. Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI+] and [URE3].

Original languageEnglish
Article numberPMID: 28932898
Pages (from-to)317-325
Number of pages9
JournalCurrent Genetics
Volume64
Issue number2
DOIs
Publication statusPublished - 1 Apr 2018

Fingerprint

Prions
Yeasts
Amyloid
Molecular Chaperones
Cell Division
Cytosol

Scopus subject areas

  • Genetics

Cite this

@article{17f44d5cdb754501aa34982abd2f304b,
title = "Differential effects of chaperones on yeast prions: CURrent view",
abstract = "Endogenous yeast amyloids that control heritable traits and are frequently used as models for human amyloid diseases are termed yeast prions. Yeast prions, including the best studied ones ([PSI+] and [URE3]), propagate via intimate interactions with molecular chaperones. Different yeast prions exhibit differential responses to changes in levels, functionality or localization of the components of chaperone machinery. Here, we provide additional data confirming differential effects of chaperones (and specifically, Hsp40s) on yeast prions and summarize current knowledge of the mechanisms underlying chaperone specificities. Contrary to frequent statements in literature, overproduction of the Hsp104 chaperone antagonizes both [PSI+] and [URE3] prions, while overproduction of the Hsp70-Ssa1 chaperone antagonizes [URE3] prion only in some, but not in all strains. Recently, we demonstrated that the relocalization of a fraction of the Hsp40 chaperone Sis1 from the cytosol to the nucleus by the chaperone-sorting factor Cur1 exhibits opposite effects on [PSI+] and [URE3] prions. We suggest that the response of prions to changes in Sis1 localization represents a combination of the effects of Sis1 shortage on fragmentation of prion aggregates and on malpartition of prion aggregates during a cell division. Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI+] and [URE3].",
keywords = "Cur1, Hsp40, Hsp70, Molecular chaperone, Yeast prion, CO-CHAPERONES, HSP70, VARIANTS, ELIMINATION, PROTEIN CHAPERONES, HSP104 OVEREXPRESSION, SIS1, URE3 PRION, SACCHAROMYCES-CEREVISIAE PSI+, PROPAGATION",
author = "Matveenko, {Andrew G.} and Barbitoff, {Yury A.} and Jay-Garcia, {Lina Manuela} and Chernoff, {Yury O.} and Zhouravleva, {Galina A.}",
year = "2018",
month = "4",
day = "1",
doi = "10.1007/s00294-017-0750-3",
language = "English",
volume = "64",
pages = "317--325",
journal = "Current Genetics",
issn = "0172-8083",
publisher = "Springer",
number = "2",

}

Differential effects of chaperones on yeast prions: CURrent view. / Matveenko, Andrew G.; Barbitoff, Yury A.; Jay-Garcia, Lina Manuela; Chernoff, Yury O.; Zhouravleva, Galina A.

In: Current Genetics, Vol. 64, No. 2, PMID: 28932898, 01.04.2018, p. 317-325.

Research output

TY - JOUR

T1 - Differential effects of chaperones on yeast prions: CURrent view

AU - Matveenko, Andrew G.

AU - Barbitoff, Yury A.

AU - Jay-Garcia, Lina Manuela

AU - Chernoff, Yury O.

AU - Zhouravleva, Galina A.

PY - 2018/4/1

Y1 - 2018/4/1

N2 - Endogenous yeast amyloids that control heritable traits and are frequently used as models for human amyloid diseases are termed yeast prions. Yeast prions, including the best studied ones ([PSI+] and [URE3]), propagate via intimate interactions with molecular chaperones. Different yeast prions exhibit differential responses to changes in levels, functionality or localization of the components of chaperone machinery. Here, we provide additional data confirming differential effects of chaperones (and specifically, Hsp40s) on yeast prions and summarize current knowledge of the mechanisms underlying chaperone specificities. Contrary to frequent statements in literature, overproduction of the Hsp104 chaperone antagonizes both [PSI+] and [URE3] prions, while overproduction of the Hsp70-Ssa1 chaperone antagonizes [URE3] prion only in some, but not in all strains. Recently, we demonstrated that the relocalization of a fraction of the Hsp40 chaperone Sis1 from the cytosol to the nucleus by the chaperone-sorting factor Cur1 exhibits opposite effects on [PSI+] and [URE3] prions. We suggest that the response of prions to changes in Sis1 localization represents a combination of the effects of Sis1 shortage on fragmentation of prion aggregates and on malpartition of prion aggregates during a cell division. Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI+] and [URE3].

AB - Endogenous yeast amyloids that control heritable traits and are frequently used as models for human amyloid diseases are termed yeast prions. Yeast prions, including the best studied ones ([PSI+] and [URE3]), propagate via intimate interactions with molecular chaperones. Different yeast prions exhibit differential responses to changes in levels, functionality or localization of the components of chaperone machinery. Here, we provide additional data confirming differential effects of chaperones (and specifically, Hsp40s) on yeast prions and summarize current knowledge of the mechanisms underlying chaperone specificities. Contrary to frequent statements in literature, overproduction of the Hsp104 chaperone antagonizes both [PSI+] and [URE3] prions, while overproduction of the Hsp70-Ssa1 chaperone antagonizes [URE3] prion only in some, but not in all strains. Recently, we demonstrated that the relocalization of a fraction of the Hsp40 chaperone Sis1 from the cytosol to the nucleus by the chaperone-sorting factor Cur1 exhibits opposite effects on [PSI+] and [URE3] prions. We suggest that the response of prions to changes in Sis1 localization represents a combination of the effects of Sis1 shortage on fragmentation of prion aggregates and on malpartition of prion aggregates during a cell division. Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI+] and [URE3].

KW - Cur1

KW - Hsp40

KW - Hsp70

KW - Molecular chaperone

KW - Yeast prion

KW - CO-CHAPERONES

KW - HSP70

KW - VARIANTS

KW - ELIMINATION

KW - PROTEIN CHAPERONES

KW - HSP104 OVEREXPRESSION

KW - SIS1

KW - URE3 PRION

KW - SACCHAROMYCES-CEREVISIAE PSI+

KW - PROPAGATION

UR - http://www.scopus.com/inward/record.url?scp=85029606805&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/differential-effects-chaperones-yeast-prions-current-view

U2 - 10.1007/s00294-017-0750-3

DO - 10.1007/s00294-017-0750-3

M3 - Review article

AN - SCOPUS:85029606805

VL - 64

SP - 317

EP - 325

JO - Current Genetics

JF - Current Genetics

SN - 0172-8083

IS - 2

M1 - PMID: 28932898

ER -