Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance
| Autor: | Anthony Guihur, Pierre Goloubinoff, Bruno Fauvet, Andrija Finka, Manfredo Quadroni |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Proteomics
Thermotolerance 0106 biological sciences 0301 basic medicine Programmed cell death Physiology Physcomitrium Plant Science Protein aggregation 01 natural sciences Workflow 03 medical and health sciences Cytosol heat‐shock response molecular crowding Gene Expression Regulation Plant Tandem Mass Spectrometry Heat shock protein heat-priming heat-shock proteins heat-shock response HSP20s-heat-shock proteins molecular crowding Physcomitrium patens proteomics RNA-Seq thermotolerance Physcomitrium patens RNA‐Seq HSP20 Heat-Shock Proteins Heat shock Heat-Shock Proteins heat‐priming Plant Proteins biology HSP20s-heat-shock proteins RNA-Seq heat-priming heat-shock proteins heat-shock response proteomics thermotolerance HSP20s‐heat‐shock proteins Photosystem II Protein Complex biology.organism_classification Bryopsida Cell biology Chloroplast heat‐shock proteins 030104 developmental biology Multiprotein Complexes Original Article Chromatography Liquid Molecular Chaperones 010606 plant biology & botany |
| Zdroj: | Plant, cell & environment, vol. 44, no. 7, pp. 2117-2133 Plant, Cell & Environment |
| Popis: | 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. Quantitative proteomics showed that a mild heat pre‐treatment leading to acquired thermotolerance in moss strongly induces the accumulation of cytosolic HSP20s, albeit in low amounts compared to other HSPs. The cytosol was found to be the least crowded cellular compartment, suggesting that in addition to their general anti‐aggregation function, cytosolic HSP20s carry specific signalling functions to regulate noxious heat‐induced apoptosis. |
| Databáze: | OpenAIRE |
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