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Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii

KEY MESSAGE: We have identified 39 proteins that interact directly or indirectly with high confidence with chloroplast HSP22E/F under heat stress thus revealing chloroplast processes affected by heat. ABSTRACT: Under conditions promoting protein unfolding, small heat shock proteins (sHsps) prevent t...

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Autores principales: Rütgers, Mark, Muranaka, Ligia Segatto, Mühlhaus, Timo, Sommer, Frederik, Thoms, Sylvia, Schurig, Juliane, Willmund, Felix, Schulz-Raffelt, Miriam, Schroda, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5700999/
https://www.ncbi.nlm.nih.gov/pubmed/29094278
http://dx.doi.org/10.1007/s11103-017-0672-y
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author Rütgers, Mark
Muranaka, Ligia Segatto
Mühlhaus, Timo
Sommer, Frederik
Thoms, Sylvia
Schurig, Juliane
Willmund, Felix
Schulz-Raffelt, Miriam
Schroda, Michael
author_facet Rütgers, Mark
Muranaka, Ligia Segatto
Mühlhaus, Timo
Sommer, Frederik
Thoms, Sylvia
Schurig, Juliane
Willmund, Felix
Schulz-Raffelt, Miriam
Schroda, Michael
author_sort Rütgers, Mark
collection PubMed
description KEY MESSAGE: We have identified 39 proteins that interact directly or indirectly with high confidence with chloroplast HSP22E/F under heat stress thus revealing chloroplast processes affected by heat. ABSTRACT: Under conditions promoting protein unfolding, small heat shock proteins (sHsps) prevent the irreversible aggregation of unfolding proteins by integrating into forming aggregates. Aggregates containing sHsps facilitate the access of Hsp70 and ClpB/Hsp104 chaperones, which in ATP-dependent reactions disentangle individual proteins from the aggregates and assist in their refolding to the native state. Chlamydomonas reinhardtii encodes eight different sHsps (HSP22A to H). The goal of this work was to identify chloroplast-targeted sHsps in Chlamydomonas and to obtain a comprehensive list of the substrates with which they interact during heat stress in order to understand which chloroplast processes are disturbed under heat stress. We show that HSP22E and HSP22F are major chloroplast-targeted sHsps that have emerged from a recent gene duplication event resulting from the ongoing diversification of sHsps in the Volvocales. HSP22E/F strongly accumulate during heat stress and form high molecular mass complexes. Using differential immunoprecipitation, mass spectrometry and a stringent filtering algorithm we identified 39 proteins that with high-confidence interact directly or indirectly with HSP22E/F under heat stress. We propose that the apparent thermolability of several of these proteins might be a desired trait as part of a mechanism enabling Chlamydomonas chloroplasts to rapidly react to thermal stress. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s11103-017-0672-y) contains supplementary material, which is available to authorized users.
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spelling pubmed-57009992017-12-04 Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii Rütgers, Mark Muranaka, Ligia Segatto Mühlhaus, Timo Sommer, Frederik Thoms, Sylvia Schurig, Juliane Willmund, Felix Schulz-Raffelt, Miriam Schroda, Michael Plant Mol Biol Article KEY MESSAGE: We have identified 39 proteins that interact directly or indirectly with high confidence with chloroplast HSP22E/F under heat stress thus revealing chloroplast processes affected by heat. ABSTRACT: Under conditions promoting protein unfolding, small heat shock proteins (sHsps) prevent the irreversible aggregation of unfolding proteins by integrating into forming aggregates. Aggregates containing sHsps facilitate the access of Hsp70 and ClpB/Hsp104 chaperones, which in ATP-dependent reactions disentangle individual proteins from the aggregates and assist in their refolding to the native state. Chlamydomonas reinhardtii encodes eight different sHsps (HSP22A to H). The goal of this work was to identify chloroplast-targeted sHsps in Chlamydomonas and to obtain a comprehensive list of the substrates with which they interact during heat stress in order to understand which chloroplast processes are disturbed under heat stress. We show that HSP22E and HSP22F are major chloroplast-targeted sHsps that have emerged from a recent gene duplication event resulting from the ongoing diversification of sHsps in the Volvocales. HSP22E/F strongly accumulate during heat stress and form high molecular mass complexes. Using differential immunoprecipitation, mass spectrometry and a stringent filtering algorithm we identified 39 proteins that with high-confidence interact directly or indirectly with HSP22E/F under heat stress. We propose that the apparent thermolability of several of these proteins might be a desired trait as part of a mechanism enabling Chlamydomonas chloroplasts to rapidly react to thermal stress. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s11103-017-0672-y) contains supplementary material, which is available to authorized users. Springer Netherlands 2017-11-01 2017 /pmc/articles/PMC5700999/ /pubmed/29094278 http://dx.doi.org/10.1007/s11103-017-0672-y 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 Article
Rütgers, Mark
Muranaka, Ligia Segatto
Mühlhaus, Timo
Sommer, Frederik
Thoms, Sylvia
Schurig, Juliane
Willmund, Felix
Schulz-Raffelt, Miriam
Schroda, Michael
Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title_full Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title_fullStr Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title_full_unstemmed Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title_short Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii
title_sort substrates of the chloroplast small heat shock proteins 22e/f point to thermolability as a regulative switch for heat acclimation in chlamydomonas reinhardtii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5700999/
https://www.ncbi.nlm.nih.gov/pubmed/29094278
http://dx.doi.org/10.1007/s11103-017-0672-y
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