Cereal Research Communications

, Volume 41, Issue 1, pp 78–87 | Cite as

The Proteome Response of Hordeum spontaneum to Salinity Stress

  • F. FatehiEmail author
  • A. Hosseinzadeh
  • H. Alizadeh
  • T. Brimavandi


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).


Hordeum spontaneum proteomics salinity two-dimensional gel electrophoresis 


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© Akadémiai Kiadó, Budapest 2013

This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, 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.

Authors and Affiliations

  • F. Fatehi
    • 1
    Email author
  • A. Hosseinzadeh
    • 1
  • H. Alizadeh
    • 1
  • T. Brimavandi
    • 2
  1. 1.Department of Agronomy and Plant BreedingUniversity of TehranKarajIran
  2. 2.Department of Food Science and Technology, Faculty of AgricultureIslamic Azad UniversityTehranIran

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