Expression of calmodulin and lipid transfer protein genes in Prunus incisa x serrula under different stress conditions
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Updated: Jun 25, 2026

Measuring Spatial and Temporal Ca2+ Signals in Arabidopsis Plants
Published on: September 2, 2014
Fatemeh Maghuly1, Eduviges G Borroto-Fernandez, Mahmood A Khan
1Plant Biotechnology Unit, Biotechnology Department, BOKU University, Muthgasse 18, 1190 Vienna, Austria.
Abstract:
Calcium-binding proteins and pathogenesis-related (PR) proteins are crucial components of the inducible repertoire of plant stress and defence. Considering the important role played by calmodulin (CaM) and lipid transfer protein (LTP) in mediating plant signal transduction, the present study investigated the expression of Ltp and CaM genes in Prunus incisa x serrula (PIS) under various abiotic stress conditions. The aim of this study is to find out whether expression of these proteins is regulated in parallel or independently and to compare the expression profiles of CaM and allergenic proteins like Ltp under different stress conditions. Southern blot analyses indicated that Ltp and CaM are encoded by at least two to four genes, which might be indicative for the expected variability and presence of isoforms. Transcription levels of both genes were analysed in leaves and roots of micropropagated plantlets under low and high temperatures, salicylic acid and wounding stress, harvested after 0, 0.5, 1, 2, 4, 10, 24 and 72 h. Real Time qPCR data showed that both genes respond differently to various stresses. Furthermore, a high variation in transcription levels of both genes was observed in leaf tissues, while in roots both genes were expressed at a lower extent and down-regulated. Western blot analyses indicated that after 24 h the amount of CaM protein is higher, while the amount of LTP is lower in various stresses. Results obtained suggest that CaM and LTP are differentially regulated in response to different stresses in PIS plants, and additionally show tissue-specific expression, hinting at a potential role of different isoforms.
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