Cargando…

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat‐labile membranes and proteins functional. A gradual morning pre‐exposure to increasing sub‐damaging temperatures induces heat‐shock protein...

Descripción completa

Detalles Bibliográficos
Autores principales: Guihur, Anthony, Fauvet, Bruno, Finka, Andrija, Quadroni, Manfredo, Goloubinoff, Pierre
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Ltd. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8359368/
https://www.ncbi.nlm.nih.gov/pubmed/33314263
http://dx.doi.org/10.1111/pce.13975
_version_ 1783737533760274432
author Guihur, Anthony
Fauvet, Bruno
Finka, Andrija
Quadroni, Manfredo
Goloubinoff, Pierre
author_facet Guihur, Anthony
Fauvet, Bruno
Finka, Andrija
Quadroni, Manfredo
Goloubinoff, Pierre
author_sort Guihur, Anthony
collection PubMed
description At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat‐labile membranes and proteins functional. A gradual morning pre‐exposure to increasing sub‐damaging temperatures induces heat‐shock proteins (HSPs) that are central to the onset of plant acquired thermotolerance (AT). To gain knowledge on the mechanisms of AT in the model land plant Physcomitrium patens, we used label‐free LC–MS/MS proteomics to quantify the accumulated and depleted proteins before and following a mild heat‐priming treatment. High protein crowding is thought to promote protein aggregation, whereas molecular chaperones prevent and actively revert aggregation. Yet, we found that heat priming (HP) did not accumulate HSP chaperones in chloroplasts, although protein crowding was six times higher than in the cytosol. In contrast, several HSP20s strongly accumulated in the cytosol, yet contributing merely 4% of the net mass increase of heat‐accumulated proteins. This is in poor concordance with their presumed role at preventing the aggregation of heat‐labile proteins. The data suggests that under mild HP unlikely to affect protein stability. Accumulating HSP20s leading to AT, regulate the activity of rare and specific signalling proteins, thereby preventing cell death under noxious heat stress.
format Online
Article
Text
id pubmed-8359368
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher John Wiley & Sons, Ltd.
record_format MEDLINE/PubMed
spelling pubmed-83593682021-08-17 Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance Guihur, Anthony Fauvet, Bruno Finka, Andrija Quadroni, Manfredo Goloubinoff, Pierre Plant Cell Environ Original Article At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat‐labile membranes and proteins functional. A gradual morning pre‐exposure to increasing sub‐damaging temperatures induces heat‐shock proteins (HSPs) that are central to the onset of plant acquired thermotolerance (AT). To gain knowledge on the mechanisms of AT in the model land plant Physcomitrium patens, we used label‐free LC–MS/MS proteomics to quantify the accumulated and depleted proteins before and following a mild heat‐priming treatment. High protein crowding is thought to promote protein aggregation, whereas molecular chaperones prevent and actively revert aggregation. Yet, we found that heat priming (HP) did not accumulate HSP chaperones in chloroplasts, although protein crowding was six times higher than in the cytosol. In contrast, several HSP20s strongly accumulated in the cytosol, yet contributing merely 4% of the net mass increase of heat‐accumulated proteins. This is in poor concordance with their presumed role at preventing the aggregation of heat‐labile proteins. The data suggests that under mild HP unlikely to affect protein stability. Accumulating HSP20s leading to AT, regulate the activity of rare and specific signalling proteins, thereby preventing cell death under noxious heat stress. John Wiley & Sons, Ltd. 2020-12-21 2021-07 /pmc/articles/PMC8359368/ /pubmed/33314263 http://dx.doi.org/10.1111/pce.13975 Text en © 2020 The Authors. Plant, Cell & Environment published by John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Original Article
Guihur, Anthony
Fauvet, Bruno
Finka, Andrija
Quadroni, Manfredo
Goloubinoff, Pierre
Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title_full Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title_fullStr Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title_full_unstemmed Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title_short Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
title_sort quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8359368/
https://www.ncbi.nlm.nih.gov/pubmed/33314263
http://dx.doi.org/10.1111/pce.13975
work_keys_str_mv AT guihuranthony quantitativeproteomicanalysistocapturetheroleofheataccumulatedproteinsinmossplantacquiredthermotolerance
AT fauvetbruno quantitativeproteomicanalysistocapturetheroleofheataccumulatedproteinsinmossplantacquiredthermotolerance
AT finkaandrija quantitativeproteomicanalysistocapturetheroleofheataccumulatedproteinsinmossplantacquiredthermotolerance
AT quadronimanfredo quantitativeproteomicanalysistocapturetheroleofheataccumulatedproteinsinmossplantacquiredthermotolerance
AT goloubinoffpierre quantitativeproteomicanalysistocapturetheroleofheataccumulatedproteinsinmossplantacquiredthermotolerance