Plasma membrane ATPase and the aquaporin HvPIP1 in barley brassinosteroid mutants acclimated to high and low temperature
| Autor: | Damian Gruszka, Iwona Sadura, Marta Libik-Konieczny, Barbara Jurczyk, Anna Janeczko |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Hot Temperature Physiology Acclimatization ATPase Mutant Cell Aquaporin HvPIP1 Plant Science Aquaporins High temperatures 01 natural sciences 03 medical and health sciences chemistry.chemical_compound Brassinosteroids medicine Brassinosteroid Low temperatures Plant Proteins Adenosine Triphosphatases biology Chemistry Hordeum PM H+-ATPase Cold Temperature 030104 developmental biology Membrane medicine.anatomical_structure Membrane protein Biochemistry Mutation biology.protein Agronomy and Crop Science Acclimation 010606 plant biology & botany |
| Popis: | The integral parts of the cell membranes are the functional proteins, which are crucial for cell life. Among them, proton-pumping ATPase and aquaporins appear to be of particular importance. There is some knowledge about the effect of the temperature during plant growth, including stress-inducing temperatures, on the accumulation of the membrane proteins: plasma membrane H+-ATPase and aquaporins, but not much is known about the effect of the phytohormones (i.e. brassinosteroids (BR)) on control of accumulation of these proteins. The aim of our study was to answer the question of how a BR deficit and disturbances in the BR perception/signalling affect the accumulation of plasma membrane H+-ATPase (PM H+-ATPase), the aquaporin HvPIP1 transcript and protein in barley growing at 20 °C and during its acclimation at 5 °C and 27 °C. For the studies, the BR-deficient mutant 522DK (derived from the wild-type Delisa), the BR-deficient mutant BW084 and the BR-signalling mutant BW312 and their wild-type Bowman were used. Generally, temperature of growth was significant factor influencing on the level of the accumulation of the H+-ATPase and HvPIP1 transcript and the PM H+-ATPase and HvPIP1 protein in barley leaves. The level of the accumulation of the HvPIP1 transcript decreased at 5 °C (compared to 20 °C), but was higher at 27 °C than at 20 °C in the analyzed cultivars. In both cultivars the protein HvPIP1 was accumulated in the highest amounts at 27 °C. On the other hand, the barley mutants with a BR deficiency or with BR signalling disturbances were characterised by an altered accumulation level of PM H+-ATPase, the aquaporin HvPIP1 transcript and protein (compared to the wild types), which may suggest the involvement of brassinosteroids in regulating PM H+-ATPase and aquaporin HvPIP1 at the transcriptional and translational levels. |
| Databáze: | OpenAIRE |
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