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

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• 作者：Chunmiao Jiang (1) (2)
  Zaiquan Cheng (2)
  Cheng Zhang (1)
  Tengqiong Yu (2)
  Qiaofang Zhong (2)
  J Qingxi Shen (3)
  Xingqi Huang (1) (2)
  
  1. College of Life Science ; Yunnan University ; Kunming ; Yunnan ; 650031 ; P.R. China
  2. Biotechnology & Genetic Germplasm Institute ; Yunnan Academy of Agricultural Sciences ; Kunming ; Yunnan ; 650223 ; P.R. China
  3. School of Life Science ; University of Nevada ; Las vegas ; USA
  
• 关键词：Wild rice species ; Seed storage proteins ; Glutelin acidic subunits ; 2 ; DE ; LC/ESI ; MS/MS ; Nutritional quality
• 刊名：Proteome Science
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：12
• 期：1
• 全文大小：1,119 KB
• 参考文献：1. Khush, GS (1997) Origin, dispersal, cultivation and variation of rice. Plant Mol Biol 35: pp. 25-34 CrossRef
  2. Osborne, TB (1924) The Vegetable Proteins. Longmans, Green, London
  3. Kawakatsu, T, Yamamoto, MP, Hirose, S, Yano, M, Takaiwa, F (2008) Characterization of a new rice glutelin gene GluD-1 expressed in the starchy endosperm. J Exp Bot 59: pp. 4223-4245 CrossRef
  4. Yamagata, H, Sugimoto, T, Tanaka, K, Kasai, Z (1982) Biosynthesis of storage proteins in developing rice seeds. Plant Physiol 70: pp. 1094-1100 CrossRef
  5. Sarker, SC, Ogawa, M, Takahashi, M, Asada, K (1986) The processing of a 57-kDa precursor peptide to subunits of rice glutelin. Plant Cell Physiol 27: pp. 1579-1586
  6. Ogawa, M, Kumamaru, T, Satoh, H, Iwata, N, Omura, T, Kasai, Z, Tanaka, K (1987) Purification of protein body-I of rice seed and its polypeptide composition. Plant Cell Physiol 28: pp. 1517-1527
  7. Kumamaru, T, Satoh, H, Iwata, N, Omura, T, Omura, T, Ogawa, M, Tanaka, K (1988) Mutants for rice storage proteins I: screening of mutants for rice storage proteins of protein bodies in the starchy endosperm. Theor Appl Genet 76: pp. 11-16 CrossRef
  8. Lin, SK, Chang, MC, Tsai, YG, Lur, HS (2005) Proteomic analysis of the expression of proteins related to rice quality during caryopsis development and the effect of high temperature on expression. Proteomics 5: pp. 2140-2156 CrossRef
  9. Katsube-Tanaka T, Khan N, Iida S, Yamaguchi T, Nakano J, Tsujimoto H: 鈥淩ecognizing Past Achievements, Meeting Future Needs!鈥? In / Proceedings of the 5th International Crop Science Congress. Jeju, Korea: 2008. www.cropscience2008.com.
  10. Cheng, ZQ, Huang, XQ, Zhang, YZ, Qian, J, Yang, MZ, Wu, CJ, Liu, JF (2005) Diversity in the content of some nutritional components in husked seeds of three wild rice species and rice varieties in Yunnan Province of China. J Integr Plant Biol 47: pp. 1260-1270 CrossRef
  11. Finnie, C, Melchior, S, Roepstorff, P, Svensson, B (2002) Proteome analysis of grain filling and seed maturation in Barley. Plant Physiol 129: pp. 1308-1319 CrossRef
  12. Xie, ZS, Wang, JQ, Cao, ML, Zhao, CF, Zhao, K, Shao, JM, Lei, TT, Xu, NZ, Liu, SQ (2006) Pedigree analysis of an elite rice hybrid using proteomic approach. Proteomics 6: pp. 474-486 CrossRef
  13. Komatsu, S, Tanaka, N (2004) Rice proteome analysis: A step toward functional analysis of the rice genome. Proteomics 4: pp. 938-949
  14. Shewry, PR (2007) Improving the protein content and composition of cereal grain. J Cereal Sci 46: pp. 239-250 CrossRef
  15. Tanaka, Y, Hayashida, S, Hongo, M (1975) The relationship of the feces protein particles to rice protein bodies. Agric Biol Chem 39: pp. 515-518 CrossRef
  16. Krishnan, HB, White, JA, Pueppke, SG (1992) Characterization and localiza tion of rice (Oryza Sativa L.) seed globulins. Plant Sci 81: pp. 1-11 CrossRef
  17. Ashida, K, Iida, S, Yasui, T (2006) Lack of 26 kDa globulin accompanies increased free amino acid content in rice (Oryza sativa L.) grains. J Cereal Sci 43: pp. 387-392 CrossRef
  18. Iida, S, Amano, E, Nishio, T (1993) A rice (Oryza sativa L.) mutant having a low content of glutelin and a high content of prolamine. Theor Appl Genet 87: pp. 374-378 CrossRef
  19. Iida, S, Kusaba, M, Nishio, T (1997) Mutants lacking glutelin subunits in rice: mapping and combination of mutated glutelin genes. Theor Appl Genet 94: pp. 177-183 CrossRef
  20. Qu, LQ, Wei, XL, Satoh, H, Kumamaru, T, Ogawa, M, Jia, X (2001) New rice mutants lacking glutelin伪-1 subunit. Acta Genetic Sinica 28: pp. 229-235
  21. Bradford, MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal Biochem 72: pp. 248-254 CrossRef
  22. Candiano, G, Bruschi, M, Musante, L, Santucci, L, Ghiggeri, G, Carnemolla, B, Orecchia, P, Zardi, L, Righetti, P (2004) Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25: pp. 1327-1333 CrossRef
  
• 刊物主题：Proteomics;
• 出版者：BioMed Central
• ISSN：1477-5956

文摘

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.