DOI QR코드

DOI QR Code

A Systematic Proteome Study of Seed Storage Proteins from Two Soybean Genotypes

  • Cho, Seong-Woo (Department of Crop Science, Chungbuk National University) ;
  • Kwon, Soo-Jeong (Department of Crop Science, Chungbuk National University) ;
  • Roy, Swapan Kumar (Department of Crop Science, Chungbuk National University) ;
  • Kim, Hong-Sig (Department of Crop Science, Chungbuk National University) ;
  • Lee, Chul-Won (Department of Crop Science, Chungbuk National University) ;
  • Woo, Sun Hee (Department of Crop Science, Chungbuk National University)
  • Received : 2014.08.19
  • Accepted : 2014.08.25
  • Published : 2014.09.30

Abstract

Soybean seed is a good source of plant protein in human consumables such as baby formula and protein concentrate. The seeds contain an abundance of storage proteins, namely ${\beta}$-conglycin and glycinin that account for ~ 70-80% of the total seed protein content. Proteome profiling has been proved to be an efficient way that can help us to investigate the seed storage proteins. In the present study, the seeds were removed from the pods and the cotylendonary tissues were separated from the testa for proteome analysis in order to investigate the seed storage proteins. A systematic proteome profiling was conducted through one-dimensional gel electrophoresis followed by MALDI-TOF-TOF mass spectrometry in the seeds (cotyledonary tissue) of soybean genotypes. Two dimensional gels stained with CBB, a total of 10 proteins were identified and analyzed using MASCOT search engine according to the similarity of sequences with previously characterized proteins along with the UniProt database. A total of ten proteins such as glycinin Gy4 precursor, glycinin G3 precursor, glycinin G1 precursor, glycinin chain A2B1a precursor, glycinin chain A2B1a precursor were identified in our investigation. However, the glycinin subunit may be considered to play important roles in soybean breeding and biochemical characterization. In addition, the improved technique will be useful to dissect the genetic control of glycinin expression in soybean.

Keywords

References

  1. Ereken-Tumer, N., J. D. Richer, and N. C. Nielsen. 1982. J. Biol. Chem. 257 : 4016-4018.
  2. Harada J. J., S. J. Barker, and R. B. Goldberg. 1989. Soybean ${\beta}$-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and post-transcriptional processes. Plant Cell 1 : 415-425.
  3. Harada, K., Y. Toyokawa, and K. Kitamura. 1983. Genetic analysis of the most acidic 11S globulin subunit and related characters in soybean seeds. Jpn. J. Breed. 33(1) : 23-33. https://doi.org/10.1270/jsbbs1951.33.23
  4. Herman E. M. and B. A. Larkins. 1999. Protein storage bodies and vacuoles. Plant Cell 11 : 601-614. https://doi.org/10.1105/tpc.11.4.601
  5. Hirano, T. O. S. H. I. O., K. O. U. J. I. Fujimoto, T. S. U. Y. O. S. H. I. Teranishi, N. A. O. K. I. Nishino, K. Onoue, S. Maeda, and K. Shimada. 1984. Phorbol ester increases the level of interleukin 2 mRNA in mitogen-stimulated human lymphocytes. J. Immunol. 132(5) : 2165-2167.
  6. Natarajan, S. S., H. B. Krishnan, F. Khan, X. Chen, W. M. Garrett, and D. Lakshman. 2013. Analysis of soybean embryonic axis proteins by two-dimensional gel electrophoresis and mass spectrometry. J. Basic Applied Sci. 9 : 302-308.
  7. Natarajan, S., C. Xu, H. Bae, B. A. Bailey, P. Cregan, Caperna, J. C. Thomas, M. G. Wesley, and L. Devanand. 2007. Proteomic and genetic analysis of glycinin subunits of sixteen soybean genotypes. Plant physiol. Biochem. 45(6) : 436-444. https://doi.org/10.1016/j.plaphy.2007.03.031
  8. Nielsen N. C., C. D. Dickinson, T. J. Cho, V. H. Thanh, and B. J. Scallon. 1989. Characterization of the glycinin gene family in soybean. Plant Cell 1 : 313-328. https://doi.org/10.1105/tpc.1.3.313
  9. Nielsen N. C., C. D. Dickinson, T. J. Cho, V. H. Thanh, B. J. Scallon, R. L. Fischer, T. L. Sims, G. N. Drews, and R. B. Goldberg. 1989. Characterization of the glycinin gene family in soybean. Plant Cell 1 : 313-328. https://doi.org/10.1105/tpc.1.3.313
  10. Nielson, N. C. 1985. The structure and complexity of the 11S polypeptide in soybean. J. Am. Oil Chem. 49 : 2733-2740.
  11. O'Farrell, P. H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250 : 4007-4021.
  12. Odanaka, H. and N. Kaizuma. 1987. Mutants on soybean storage protein induced with r-ray irradiation (in Japanese). Jpn. J. Breed. 39(Suppl. 1) : 430-431.
  13. Schmidt, M. A., W. B. Barbazuk, M. Sandford, G. May, Z. Song, W. Zhou, and E. M. Herman. 2011. Silencing of soybean seed storage proteins results in a rebalanced protein composition preserving seed protein content without major collateral changes in the metabolome and transcriptome. Plant physiol. 156(1) : 330-345. https://doi.org/10.1104/pp.111.173807
  14. Schuler M. A., B. F. Ladin, G. Fryer, J. G. Pollaco, and R. N. Beachy. 1982a. Structural sequences are conserved in the genes coding for the alpha, alpha' and beta-subunits of the soybean seed storage protein and other seed proteins. Nucleic Acids Res. 10 : 8245-8260. https://doi.org/10.1093/nar/10.24.8245
  15. Schuler M. A., E. S. Schmitt, and R. N. Beachy. 1982b. Closely related families of genes code for the alpha and alpha' subunits of the soybean 7S storage protein complex. Nucleic Acids Res. 10 : 8225-8244. https://doi.org/10.1093/nar/10.24.8225
  16. Staswick, P. E., P. Broue, and N. C. Nielsen. 1983. Glycinin composition of several perennial species related to soybean. Plant physiol. 72(4) : 1114-1118. https://doi.org/10.1104/pp.72.4.1114
  17. Staswick, P. E., M. A. Hermodson, and N. C. Nielsen. 1984. Identification of the cystines which link the acidic and basic components of the glycinin subunit. J. Biol. Chem. 259 : 13431-13435.

Cited by

  1. Analysis of Protein Function and Comparison of Protein Expression of Different Environment in Soybean using Proteomics Techniques vol.60, pp.1, 2015, https://doi.org/10.7740/kjcs.2014.60.1.033
  2. Characterization of Protein Function and Differential Protein Expression in Soybean under Soaking Condition vol.60, pp.1, 2015, https://doi.org/10.7740/kjcs.2014.60.1.114