ArticlePlant molecular biology2017
Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii.
Article in Plant molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
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- Integrating proteomic and phosphoproteomic profiles provide new insights into ABA-dependent signal regulation network in maize response to heat stress.BMC plant biology · 2025Article
- A subfamily of the small heat shock proteins of the marine red alga Neopyropia yezoensis localizes in the chloroplast.Cell stress & chaperones · 2023Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- CLPB3 is required for the removal of chloroplast protein aggregates and thermotolerance in Chlamydomonas.Journal of experimental botany · 2023Article
- A Cyanophage MarR-Type Transcription Factor Regulates Host RNase E Expression during Infection.Microorganisms · 2022Article
- SiHSFA2e regulated expression of SisHSP21.9 maintains chloroplast proteome integrity under high temperature stress.Cellular and molecular life sciences : CMLS · 2022Article
- Systems-wide analysis revealed shared and unique responses to moderate and acute high temperatures in the green alga Chlamydomonas reinhardtii.Communications biology · 2022Article
- Fast and global reorganization of the chloroplast protein biogenesis network during heat acclimation.The Plant cell · 2022Article
- Fatty acid export (FAX) proteins contribute to oil production in the green microalgaFrontiers in molecular biosciences · 2022Article
- Progress in Research on the Mechanisms Underlying Chloroplast-Involved Heat Tolerance in Plants.Genes · 2021Review
- Hot topic: Thermosensing in plants.Plant, cell & environment · 2021Review
- Orchestral manoeuvres in the light: crosstalk needed for regulation of the Chlamydomonas carbon concentration mechanism.Journal of experimental botany · 2021Review
- Structural and functional properties of proteins interacting with small heat shock proteins.Cell stress & chaperones · 2020Review
- ThePlant physiology · 2019Article
- The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response.eLife · 2019Article
- The Role of Plastidic Trigger Factor Serving Protein Biogenesis in Green Algae and Land Plants.Plant physiology · 2019Article
- A Musashi Splice Variant and Its Interaction Partners Influence Temperature Acclimation inPlant physiology · 2018Article
- Chloroplast Damage Induced by the Inhibition of Fatty Acid Synthesis Triggers Autophagy in Chlamydomonas.Plant physiology · 2018Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
key messageWe 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. 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.
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