Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology

• Published in: Journal of experimental botany 2006-04, Vol.57 (7), p.1537-1546
• Main Authors: Amme, Steffen, Matros, Andrea, Schlesier, Bernhard, Mock, Hans-Peter
• Format: Article
• Language: English
• Subjects: 2D gel electrophoresis; air temperature; Arabidopsis - anatomy & histology; Arabidopsis - growth & development; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; Biological and medical sciences; cold; cold stress; Cold Temperature; cold tolerance; Computer software; Dyes; Electrophoresis; Electrophoresis, Gel, Two-Dimensional - methods; Fundamental and applied biological sciences. Psychology; Gels; Genes; Mass Spectrometry; Mass spectroscopy; new methods; Physical agents; Plant physiology and development; Plants; protein composition; protein synthesis; Proteomes; Proteomics; Proteomics - methods; Vegetative apparatus, growth and morphogenesis. Senescence
• ISSN: 0022-0957; 1460-2431
• DOI: 10.1093/jxb/erj129

A proteome study based on 2-D gel electrophoresis was performed in order to analyse the cold-stress response of Arabidopsis plants. The emphasis was to monitor the overall changes in the protein complement after prolonged exposure rather than short-term responses. Two different temperature regimes were used (6 °C and 10 °C) and plants were exposed to cold-stress exposure for 1 week. Protein patterns were also monitored after re-shifting plants to control conditions for a further week. To monitor gradual changes in the response to the two cold-stress conditions, the analysis was performed with DIGE technology with the inclusion of an internal standard. In the experiments using 6 °C, 22 spots with at least 2-fold altered expression were found; among them 18 were increased and four were decreased. When plants were exposed to 10 °C, 18 of these 22 spots still showed a 2-fold change; however, the alterations were, in general, more moderate than observed under 6 °C. Spot identification was performed by MALDI-TOF and ESI-MS/MS. Many of the proteins identified have previously been described in the context of cold-stress responses, indicating the validity of this proteome approach for further in-depth studies.