Characterization of common and distinctive adjustments of wild barley leaf proteome under drought acclimation, heat stress and their combination
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In nature, plants are often exposed to combinations of different stresses at the same time, while in many laboratory studies of molecular stress induction phenomena, single stress responses are analyzed. This study aims to identify the common (i.e. more general stress-responsive) and the stress-specific adjustments of the leaf proteome of wild barley to two often co-occurring stress phenomena, i.e. in response to (long-term) drought acclimation (DA) or to (transient) heat stress (HS). In addition, we analyzed those alterations which are specific for the combination of both stresses. Leaf proteome analysis was performed using 2D difference gel electrophoresis followed by protein identification via mass spectrometry with a 1.5 threshold value of changes in relative protein contents. DA resulted in specific upregulation of proteins with cell detoxification functions, water homeostasis maintenance, amino acids synthesis and lipid metabolism and distinct forms of heat shock proteins (HSPs) and proteins with chaperon functions while proteins related to nitrogen metabolism were downregulated. This response was distinguished from the response to transient HS, which included upregulation of a broad range of HSP products. The common response to both stressors revealed upregulation of additional forms of HSPs and the downregulation of enzymes of the photosynthetic apparatus and chlorophyll binding proteins. The simultaneous exposure to both stress conditions resulted mostly in a combination of both stress responses and to unique abundance changes of proteins with yet unclear functions.
KeywordsDetoxification Difference gel electrophoresis Drought acclimation Heat shock proteins Heat stress Wild barley
Betaine aldehyde dehydrogenase
Difference gel electrophoresis
Heat shock proteins
Leaf relative water content
Matrix-assisted laser desorption/ionization
Peptide mass fingerprint
Reactive oxygen species
Small heat shock proteins
- 2D PAGE
Two dimensional polyacrylamide gel electrophoresis
Volumetric water content
This work was supported by a DAAD (German Academic Exchange Service) grant to A. Ashoub under the Alumni Re-Invitation Program.
Conflict of interest
The authors declare that they have no conflict of interest.
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