Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms

We report a large-scale plant phosphoproteome under the control of higher ambient temperature, and expose early signalling events associated with a mild temperature increase in wheat. Abstract Wheat (Triticum ssp.) is one of the most important human food sources. However, this crop is very sensitive...

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Veröffentlicht in:Journal of experimental botany 2018-08, Vol.69 (19), p.4609-4624
Hauptverfasser: Vu, Lam Dai, Zhu, Tingting, Verstraeten, Inge, van de Cotte, Brigitte, Gevaert, Kris, De Smet, Ive
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container_end_page 4624
container_issue 19
container_start_page 4609
container_title Journal of experimental botany
container_volume 69
creator Vu, Lam Dai
Zhu, Tingting
Verstraeten, Inge
van de Cotte, Brigitte
Gevaert, Kris
De Smet, Ive
description We report a large-scale plant phosphoproteome under the control of higher ambient temperature, and expose early signalling events associated with a mild temperature increase in wheat. Abstract Wheat (Triticum ssp.) is one of the most important human food sources. However, this crop is very sensitive to temperature changes. Specifically, processes during wheat leaf, flower, and seed development and photosynthesis, which all contribute to the yield of this crop, are affected by high temperature. While this has to some extent been investigated on physiological, developmental, and molecular levels, very little is known about early signalling events associated with an increase in temperature. Phosphorylation-mediated signalling mechanisms, which are quick and dynamic, are associated with plant growth and development, also under abiotic stress conditions. Therefore, we probed the impact of a short-term and mild increase in temperature on the wheat leaf and spikelet phosphoproteome. In total, 3822 (containing 5178 phosphosites) and 5581 phosphopeptides (containing 7023 phosphosites) were identified in leaf and spikelet samples, respectively. Following statistical analysis, the resulting data set provides the scientific community with a first large-scale plant phosphoproteome under the control of higher ambient temperature. This community resource on the high temperature-mediated wheat phosphoproteome will be valuable for future studies. Our analyses also revealed a core set of common proteins between leaf and spikelet, suggesting some level of conserved regulatory mechanisms. Furthermore, we observed temperature-regulated interconversion of phosphoforms, which probably impacts protein activity.
doi_str_mv 10.1093/jxb/ery204
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subjects Research Papers
title Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms
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