Proteomic analysis of the salt tolerance mutant of wheat under salt stress. Yi Chuan Xue Bao

College of Life Science, Hebei Normal University, Shijiazhuang 050016, China.
Acta Genetica Sinica 01/2005; 31(12):1408-14.
Source: PubMed


Two dimensional electrophoresis was used to analyse the proteome of the salt-tolerant mutant of wheat (RH8706-49) and the salt-sensitive mutant of wheat (H8706-34) which had been treated by 1% NaCl for 72 hours. After being analysed by MALDI-TOF-MS and Mascot software, the qualitative and quantitative differences were identified between the two materials for five candidate proteins: H+-transporting two-sector ATPase, glutamine synthetase 2 precursor, putative 33 kD oxygen evolving protein of photosystem II and ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit. These five proteins are all belong to chloroplast proteins. They are likely to play a crucial role in keeping the function of the chloroplast and the whole cells when the plant was under salt-stress.

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    • "In this study, number of Rubisco subunits was unevenly expressed in chloroplasts of water-stressed seedlings (Table 2). Isoforms of Rubisco activase likely play an important role in stabilizing and controlling proteolysis (Schwartz et al. 1995) and in maintaining chloroplast functioning during drought stress (Huo et al. 2004). Regulation of Rubisco activity has yet unclear under water stress. "
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    ABSTRACT: The performance of control and water-stressed 10-d-old wheat seedlings was compared. During short-term water stress (irrigation was withheld for 9 d), rates of photosynthesis and transpiration, stomatal conductance, and relative water content decreased whereas the proline content increased. Chloroplast proteins were extracted from the leaves, separated by iso-electric focusing through two-dimensional electrophoresis, and stained with CBB R-250. Differentially expressed proteins were detected and analyzed with MALDI-TOF/TOF mass spectrometry. Under water stress, 9 proteins were up-regulated whereas 11 proteins were not affected. The ribulose-1,5-bisphospate carboxylase/oxygenase (Rubisco) small and large subunits, chloride carrier/channel family, and H+-ATPase were up-regulated by water stress whereas membrane-bound ATP synthase subunit b and cytochrome b6-f complex were down-regulated.
    Biologia Plantarum 11/2012; 57(2). DOI:10.1007/s10535-012-0290-0 · 1.85 Impact Factor
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    • "The found drought stress up-regulates proteins in K86-161 cultivar such as protease inhibitor, RuBisCO activase isoform and ferredoxin are interesting. These proteins are likely to play a role in stabilizing, controlling proteolysis (Schwartz et al., 1995) and maintaining the function of the chloroplast during plant exposure to drought stress (Huo et al., 2004). When compared to control K86-161, the Protease inhibitor was only detected in stressed plant, thus this protein was induced by subsequent induction after stress treatment. "
    American Journal of Biochemistry and Biotechnology 04/2010; 6(2):89-102. DOI:10.3844/ajbbsp.2010.89.102
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    ABSTRACT: Soil salinity is one of the most significant abiotic stresses for crop species. Sustainable and equitable global food security is partly dependent on the development of crops and horticultural plants with increased salt tolerance. Increased salt tolerance of perennial species used for fodder or fuel production is also a key component in reducing the spread of secondary salinity in many regions in the world. New molecular '-omic' tools created major interest among researchers and opened up new perspectives in stress biology. In the last few years, considerable progress has been made in the analysis of the transcriptome to study salt stress either alone or in combination with other abiotic stresses. However, there is no review that highlights the studies conducted to-date on proteomic analysis of plant salt stress tolerance. The present review summarizes current initiatives in proteomics research for the analysis of plant salt tolerance. The first part of the review focuses on microarray studies with particular emphasis on plant salt stress tolerance. The second part deals with conceptual and technological aspects of plant proteomics in general and the analysis of salt stress tolerance in particular. The third part is a compilation of published results on proteomic analysis of plant salt tolerance and gives information on emerging technologies of plant proteomics to meet the challenges. We believe the present summary and perspective on proteomic analysis of salt stress tolerance will provide a backbone to enable further molecular dissection of salt-tolerance mechanisms and help to develop stress-tolerant plants through effective breeding strategies.
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