The Proteome Response of Hordeum spontaneum to Salinity Stress
Hordeum spontaneum (wild barley) is a good gene source to improve salt tolerance in barley because it rapidly hybridizes and recombines with barley cultivars. Proteomics can assist in identifying proteins associated with a certain environmental or developmental signal. We employed a proteomic approach to understand the mechanisms of plant responses to salinity in a salt tolerant accession of H. spontaneum. At the 4-leaf stage, wild barley plants were exposed to 0 (control treatment) or 300 mM NaCl (salt treatment). The salt treatment lasted 3 weeks. Total proteins of leaf 4 were extracted and separated by two-dimensional gel electrophoresis. More than 500 protein spots were reproducibly detected. Of these, 29 spots showed significant differences between salt treatment and control. Using MALDI-TOF-TOF MS, we identified 29 cellular proteins, which represented 16 different proteins. These were classified into six categories and a group with unknown biological function. The proteins identified were involved in many different cellular functions. Three spots were identified as unknown proteins; searching in the NCBI database revealed that there was a 71% match with clathrin assembly protein putative [Ricinus communis], a 67% match with actin binding protein [Zea mays], and a 66% match with phosphatidylinositol kinase [Arabidopsis thaliana]. Other proteins identified included ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), oxygen-evolving enhancer protein (OEE), photosystem II reaction centerWprotein (Psbw), ribosomal proteins, chloroplast RNA binding protein (ChRBP), superoxide dismutase (SOD), malate dehydrogenase (MDH), thioredoxin h (Trx), nucleoside diphosphate kinase (NDPK), profilin, translationally-controlled tumor protein (TCTP), polyamine oxidase (PAO) and universal stress protein family (USP).
KeywordsHordeum spontaneum proteomics salinity two-dimensional gel electrophoresis
Unable to display preview. Download preview PDF.
- Hajduch, M., Rakwal, R., Agrawal, G.K., Yonekura, M., Pretova, A. 2001. High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: Drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins. Electrophoresis 22:2824–2831.CrossRefGoogle Scholar
- Moon, H., Lee, B., Choi, G., Shin, D., Prasad, D.T., Lee, O., Kwak, S.S., Kim, D.H., Nam, J., Bahk, J., Hong, J.C., Lee, S.Y., Cho, M.J., Lim, C.O., Yun, D.J. 2003. NDP kinase 2 interacts with two oxidative stress-activated MAPKs to regulate cellular redox state and enhances multiple stress tolerance in transgenic plants. Proc. Natl. Acad. Sci. USA. 100:358–363.CrossRefGoogle Scholar
This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.