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Research Articles

Vol. 12 No. 2 (2025)

Sunflower (Helianthus annuus L.) seed development accompanies glycosylation and phosphorylation of total soluble and oil body membrane-associated proteins

DOI
https://doi.org/10.14719/pst.4238
Submitted
3 July 2024
Published
04-03-2025 — Updated on 01-04-2025
Versions

Abstract

Seed development is a complex process involving a series of physiological and metabolic events. During this process, glycosylation, a post-translational modification, plays a crucial role in protein targeting during cellular signaling, while protein phosphorylation acts as a molecular switch, activating proteins in the signaling cascade essential for development. Sunflower is an important oilseed crop in India and worldwide. Phosphoprotein analysis at three stages of sunflower seed development (20, 30 and 40 days after anthesis (DAA)) has revealed significant stage-specific differences in phosphoprotein and glycoprotein distribution. This analysis provides a metabolic framework for further characterizing the biochemical events associated with seed development. The present investigations will be instrumental in analysing the expression and modulation of glycosylation and phosphorylation of proteins during different phases of sunflower seed development. Additionally, this research offer insights into the regulatory roles phosphorylation and glycosylation as molecular switches in governing seed development in sunflower.

References

  1. Howell SH. Endoplasmic reticulum stress responses in plants. Annu Rev Plant Biol. 2013;64(1):477-99. https://doi.org/10.1146/annurev-arplant-050312-120053
  2. Arcalis E, Stadlmann J, Marcel S, Drakakaki G, Winter V, Rodriguez J, et al. The changing fate of a secretory glycoprotein in developing maize endosperm. Plant Physiol. 2010;153(2):693-702. https://doi.org/10.1104/pp.109.152363
  3. Basha SM, Roberts RM. The glycoproteins of plant seeds: Analysis by two-dimensional polyacrylamide gel electrophoresis and by their lectin-binding properties. Plant Physiol. 1981;67(5):936-39. https://doi.org/10.1104/pp.67.5.936
  4. Goldberg RB, Hoschek G, Vodkin LO. An insertion sequence blocks the expression of a soybean lectin gene. Cell. 1983;33(2):465-75. https://doi.org/10.1016/0092-8674(83)90428-2
  5. Okamuro JK, Jofuku KD, Goldberg RB. Soybean seed lectin gene and flanking non seed protein genes are developmentally regulated in transformed tobacco plants. Proc Natl Acad Sci. 1986;83(21):8240-44. https://doi.org/10.1073/pnas.83.21.8240
  6. Huber SC, Hardin SC. Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels. Curr Opin Plant Biol. 2004;7(3):318-22. https://doi.org/10.1016/j.pbi.2004.03.002
  7. Pawson T, Scott JD. Protein phosphorylation in signaling–50 years and counting. Trends Biochem Sci. 2005;30(6):286-90. https://doi.org/10.1016/j.tibs.2005.04.013
  8. Sugiyama N, Nakagami H, Mochida K, Daudi A, Tomita M, Shirasu K, et al. Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis. Mol Syst Biol. 2008;4(1):193. https://doi.org/10.1038/msb.2008.32
  9. Nakagami H, Sugiyama N, Mochida K, Daudi A, Yoshida Y, Toyoda T, et al. Large-scale comparative phosphoproteomics identifies conserved phosphorylation sites in plants. Plant Physiol. 2010;153(3):1161-74. https://doi.org/10.1104/pp.110.157347
  10. Grimsrud PA, den Os D, Wenger CD, Swaney DL, Schwartz D, Sussman MR, et al. Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes. Plant Physiol. 2010;152(1):19-28. https://doi.org/10.1104/pp.109.149625
  11. Kersten B, Agrawal GK, Durek P, Neigenfind J, Schulze W, Walther D, et al. Plant phosphoproteomics: An update. Proteomics. 2009;9(4):964-88. https://doi.org/10.1002/pmic.200800548
  12. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72(1-2):248-54. https://doi.org/10.1006/abio.1976.9999
  13. Markwell MA, Haas SM, Tolbert NE, Bieber LL. Protein determination in membrane and lipoprotein samples: Manual and automated procedures. Meth Enzymol Academic Press. 1981; p.296-303. https://doi.org/10.1016/S0076-6879(81)72018-4
  14. Steinberg TH. Protein gel staining methods: An introduction and overview. Meth Enzymol. 2009;463:541-63. https://doi.org/10.1016/S0076-6879(09)63031-7
  15. Kermode AR, Bewley JD. Developing seeds of Ricinus communis L., when detached and maintained in an atmosphere of high relative humidity, switch to a germinative mode without the requirement for complete desiccation. Plant Physiol. 1989;90(2):702-07. https://doi.org/10.1104/pp.90.2.702
  16. Baldoni AB, Araújo AC, de Carvalho MH, Gomes AC, Aragao FJ. Immunolocalization of ricin accumulation during castor bean (Ricinus communis L.) seed development. Int J Plant Biol. 2010;1(2):e12. https://doi.org/10.4081/pb.2010.e12
  17. Catusse J, Rajjou L, Job C, Job D. Proteome of seed development and germination. In: Agrawal GK and Rakwal R, editors. Plant proteomics: Technologies, strategies and applications. John Wiley and Sons; 2008. p. 191-206. https://doi.org/10.1002/9780470369630.ch13
  18. Ohad N, Yadegari R, Margossian L, Hannon M, Michaeli D, Harada JJ, et al. Mutations in FIE, a WD polycomb group gene, allow endosperm development without fertilization. Plant Cell. 1999;11(3):407-15. https://doi.org/10.2307/3870869
  19. Asano T, Kunieda N, Omura Y, Ibe H, Kawasaki T, Takano M, et al. Rice SPK, a calmodulin-like domain protein kinase, is required for storage product accumulation during seed development: Phosphorylation of sucrose synthase is a possible factor. Plant Cell. 2002;14(3):619-28. https://doi.org/10.1105/tpc.010454
  20. Ray S, Agarwal P, Arora R, Kapoor S, Tyagi AK. Expression analysis of calcium-dependent protein kinase gene family during reproductive development and abiotic stress conditions in rice (Oryza sativa L. ssp. indica). Mol Genet Genom. 2007;278:493-505. https://doi.org/10.1007/s00438-007-0267-4
  21. Agrawal GK, Thelen JJ. Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol Cell Proteomics. 2006;5(11):2044-59. https://doi.org/10.1074/mcp.M600084-MCP200
  22. Wan L, Ross AR, Yang J, Hegedus DD, Kermode AR. Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds. Biochem J. 2007;404(2):247-56. https://doi.org/10.1042/BJ20061569
  23. Ghelis T, Bolbach G, Clodic G, Habricot Y, Miginiac E, Sotta B, et al. Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells. Plant Physiol. 2008;148(3):1668-80. https://doi.org/10.1104/pp.108.124594
  24. Weber H, Borisjuk L, Wobus U. Molecular physiology of legume seed development. Annu Rev Plant Biol. 2005;56(1):253-79. https://doi.org/10.1146/annurev.arplant.56.032604.144201
  25. Luo M, Dennis ES, Berger F, Peacock WJ, Chaudhury A. MINISEED3 (MINI3), a WRKY family gene and HAIKU2 (IKU2), a leucine-rich repeat (LRR) KINASE gene, are regulators of seed size in Arabidopsis. Proc Natl Acad Sci USA. 2005;102(48):17531-36. https://doi.org/10.1073/pnas.0508418102
  26. Irar S, Oliveira E, Pagès M, Goday A. Towards the identification of late-embryogenic-abundant phosphoproteomics in Arabidopsis by 2-DE and MS. Proteomics. 2006;6(S1):S175-85. https://doi.org/10.1002/pmic.200500387
  27. Meyer LJ, Gao J, Xu D, Thelen JJ. Phosphoproteomics analysis of seed maturation in Arabidopsis, rapeseed and soybean. Plant physiol. 2012;159(1):517-28. https://doi.org/10.1104/pp.111.191700

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