Characterization of common and distinctive adjustments of wild barley leaf proteome under drought acclimation, heat stress and their combination

• Published in: Plant molecular biology Vol. 87; no. 4-5; pp. 459 - 471
• Main Authors: Ashoub, Ahmed, Baeumlisberger, Marion, Neupaertl, Moritz, Karas, Michael, Brüggemann, Wolfgang
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.03.2015; Springer Nature B.V
• Subjects: Abiotic stress; Barley; Biochemistry; Biomedical and Life Sciences; Drought; Droughts; Gene Expression Regulation, Plant; Heat shock proteins; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Hordeum - metabolism; Hordeum - physiology; Hot Temperature; Life Sciences; Plant biology; Plant Leaves - metabolism; Plant Leaves - physiology; Plant Pathology; Plant Proteins - genetics; Plant Proteins - metabolism; Plant Sciences; Plant tolerance; Proteomics; Heat shock proteins; Wild barley; Drought acclimation; Heat stress; Difference gel electrophoresis; Detoxification
• ISSN: 0167-4412; 1573-5028
• DOI: 10.1007/s11103-015-0291-4

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.