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Proteomic analysis of seed storage proteins in wild rice species of the Oryza genus

文献类型： 外文期刊

作者： Jiang, Chunmiao 1 ; Cheng, Zaiquan 2 ; Zhang, Cheng 1 ; Yu, Tengqiong 2 ; Zhong, Qiaofang 2 ; Shen, J. Qingxi 3 ; Huan 1 ;

作者机构： 1.Yunnan Univ, Coll Life Sci, Kunming 650031, Yunnan, Peoples R China

2.Yunnan Acad Agr Sci, Biotechnol & Genet Germplasm Inst, Kunming 650223, Yunnan, Peoples R China

3.Univ Nevada, Sch Life Sci, Las Vegas, NV 89154 USA

关键词： Wild rice species;Seed storage proteins;Glutelin acidic subunits;2-DE;LC/ESI-MS/MS;Nutritional quality

期刊名称：PROTEOME SCIENCE （ 影响因子：2.48； 五年影响因子：2.619 ）

ISSN： 1477-5956

年卷期： 2014 年 12 卷

页码：

收录情况： SCI

摘要： Background: The total protein contents of rice seeds are significantly higher in the three wild rice species (Oryza rufipogon Grill., Oryza officinalis Wall. and Oryza meyeriana Baill.) than in the cultivated rice (Oryza sativa L.). However, there is still no report regarding a systematic proteomic analysis of seed proteins in the wild rice species. Also, the relationship between the contents of seed total proteins and rice nutritional quality has not been thoroughly investigated. Results: The total seed protein contents, especially the glutelin contents, of the three wild rice species were higher than those of the two cultivated rice materials. Based on the protein banding patterns of SDS-PAGE, O. rufipogon was similar to the two cultivated rice materials, followed by O. officinalis, while O. meyeriana exhibited notable differences. Interestingly, O. meyeriana had high contents of glutelin and low contents of prolamine, and lacked 26 kDa globulin band and appeared a new 28 kDa protein band. However, for O. officinali a 16 kDa protein band was absent and a row of unique 32 kDa proteins appeared. In addition, we found that 13 kDa prolamine band disappeared while special 14 kDa and 12 kDa protein bands were present in O. officinalis. Two-dimensional gel electrophoresis (2-DE) analysis revealed remarkable differences in protein profiles of the wild rice species and the two cultivated rice materials. Also, the numbers of detected protein spots of the three wild rice species were significantly higher than those of two cultivated rice. A total of 35 differential protein spots were found for glutelin acidic subunits, glutelin precursors and glutelin basic subunits in wild rice species. Among those, 18 protein spots were specific and 17 major spots were elevated. Six differential protein spots for glutelin acidic subunits were identified, including a glutelin type-A 2 precursor and five hypothetical proteins. Conclusion: This was the first report on proteomic analysis of the three wild rice species. Overall results suggest that there were many new types of glutelin subunits and precursor in the three wild rice species. Hence, wild rice species are important genetic resources for improving nutritional quality to rice.

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