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The life of [PSI]

The AAA+ disaggregase Hsp104 is essential for the maintenance and inheritance of nearly all known prions of the yeast Saccharomyces cerevisiae. Uniquely for [PSI (+)], the prion form of the Sup35 protein, there seem to be two activities, involving differing co-chaperones, by which Hsp104 affects the...

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Detalles Bibliográficos
Autores principales: Cox, Brian, Tuite, Mick
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778180/
https://www.ncbi.nlm.nih.gov/pubmed/28653109
http://dx.doi.org/10.1007/s00294-017-0714-7
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author Cox, Brian
Tuite, Mick
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Tuite, Mick
author_sort Cox, Brian
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description The AAA+ disaggregase Hsp104 is essential for the maintenance and inheritance of nearly all known prions of the yeast Saccharomyces cerevisiae. Uniquely for [PSI (+)], the prion form of the Sup35 protein, there seem to be two activities, involving differing co-chaperones, by which Hsp104 affects the inheritance of [PSI (+)], the prion form of the Sup35 protein. Each pathway is also involved in protection against ageing, one through disaggregation of damaged proteins and the other through their retention in the mother cell during budding. Mutations in both Hsp104 and Sup35 affect prion inheritance by one or other of these pathways, as does manipulation of either Hsp104 enzyme activity or expression, in both vegetative (budding) divisions and in sporulation. Based on our recent finding (Ness et al. in Molec Microbiol 104:125–143, 2017) we suggest that the management of the heritable prion forms of Sup35 in [PSI (+)] cells in sporulation may be a marker for a role for Hsp104 in rejuvenation during sporulation.
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spelling pubmed-57781802018-02-01 The life of [PSI] Cox, Brian Tuite, Mick Curr Genet Review The AAA+ disaggregase Hsp104 is essential for the maintenance and inheritance of nearly all known prions of the yeast Saccharomyces cerevisiae. Uniquely for [PSI (+)], the prion form of the Sup35 protein, there seem to be two activities, involving differing co-chaperones, by which Hsp104 affects the inheritance of [PSI (+)], the prion form of the Sup35 protein. Each pathway is also involved in protection against ageing, one through disaggregation of damaged proteins and the other through their retention in the mother cell during budding. Mutations in both Hsp104 and Sup35 affect prion inheritance by one or other of these pathways, as does manipulation of either Hsp104 enzyme activity or expression, in both vegetative (budding) divisions and in sporulation. Based on our recent finding (Ness et al. in Molec Microbiol 104:125–143, 2017) we suggest that the management of the heritable prion forms of Sup35 in [PSI (+)] cells in sporulation may be a marker for a role for Hsp104 in rejuvenation during sporulation. Springer Berlin Heidelberg 2017-06-26 2018 /pmc/articles/PMC5778180/ /pubmed/28653109 http://dx.doi.org/10.1007/s00294-017-0714-7 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Review
Cox, Brian
Tuite, Mick
The life of [PSI]
title The life of [PSI]
title_full The life of [PSI]
title_fullStr The life of [PSI]
title_full_unstemmed The life of [PSI]
title_short The life of [PSI]
title_sort life of [psi]
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778180/
https://www.ncbi.nlm.nih.gov/pubmed/28653109
http://dx.doi.org/10.1007/s00294-017-0714-7
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