From pollen actin to crop male sterility

  • Longfei Yan
  • Guoqin Liu
  • Xingguo Xiao


Actin plays an important role in the life activity of animal and plant cells. Pollen cells have plenty of actin whose structure and characteristics are very similar to the animal actin. The nucleotide sequence and amino acid sequence of plant actin gene are very similar to those of the animal gene. The content of pollen actin from male sterile plants is much more lower than that from its maintainer plants. The expression of actin gene is organ-specific during the plant development. The expression quantity of actin gene in pollen is much more higher than those from root, stem and leaf. The expression plasmid of the anti-sense actin gene was constructed, transferred to the protoplasts of wheat and tomato to inhibit the expression of actin gene in pollen and thus the male sterile plants of wheat and tomato were obtained. The actin in pollens from the transgenic plants was reduced significantly, whereas the pistil was not affected. This study might pave a new way to breeding male sterile lines for the application of hybrid vigor of wheat and tomato.


actin pollen male sterility 


  1. 1.
    Yen, L. F., Shih, T. C., The presence of a contractile protein in higher plants, Scientia Sinica, 1965, 14(4): 601.Google Scholar
  2. 2.
    Yen, L. F., Han, Y. S., Shih, T. C., Purification of the plant contractile protein and its ATPase properties, Chin. Sci. Bull., 1966, 17(1): 138.Google Scholar
  3. 3.
    Palevitz, B. A., Ash, J. F., Hepler, P. K., Actin in the green algaNitella, Proc. Natl. Acad. Sci. USA, 1974, 71: 363.PubMedCrossRefGoogle Scholar
  4. 4.
    Williamson, R. E., Actin in the algaChara coralina, Nature, 1974, 248: 801.PubMedCrossRefGoogle Scholar
  5. 5.
    Condeelis, J. S., The identification of F-actin in the pollen tube and protoplast ofAmaryllis belledonna, Exptl. Cell. Res., 1974, 88: 435.PubMedCrossRefGoogle Scholar
  6. 6.
    Yen, L. F., Wang, X. Z., Teng, X. Y. et al., Actin and myosin in pollens and their role in the growth of pollen tubes, Chin. Sci. Bull., 1986, 31(4): 267.Google Scholar
  7. 7.
    Pierson, E. S., Derksen, J., Traas, J. A., Organization of microfilament and microtubules in pollen tubes grownin vitro orin vivo in various organism, Eur. J. Cell Biol., 1986, 41: 14.Google Scholar
  8. 8.
    Liu, G. Q., Yen, L. F., Study of the microfilament skeleton of pollen tubes, Acta Biol. Experim. Sinica, 1987, 20(2): 267.Google Scholar
  9. 9.
    Tang, X., Lancelle, S. A., Hepler, P. K., Fluorescence microscopic localization of actin in pollen tubes: Comparison of actin antibody and phalloidin staining, Cell Motil. Cytoskel., 1989, 12: 216.CrossRefGoogle Scholar
  10. 10.
    Ma, Y. Z., Yen, L. F., Comparative studies of corn pollen actin and rabbit skeletal muscle actin, Chinese Biochem. J. (in Chinese), 1989, 5(4): 320.Google Scholar
  11. 11.
    Liu, X., Yen, L. F., Purification and characterization of actin from maize pollen, Plant Physiol., 1992, 99: 1151.PubMedCrossRefGoogle Scholar
  12. 12.
    Heslop-Harrisons, J., Heslop-Hassison, Y., Myosin associated with the surface of organelles, vegetative nuclei and generative cells in angiosperm pollen grains and tubes, J. Cell Sci., 1989, 94: 319.Google Scholar
  13. 13.
    Liu, X., Yen, L. F., Organelle movement in the germinated pollen grains and pollen tubes ofOenothera odorata, Acta Botainca Sinica (in Chinese), 1993, 35(11): 859.Google Scholar
  14. 14.
    Gibbon, B. C., Ren, H., Staiger, C. J., Characterization of maize pollen profillin functionin vitro and in live cells, Plant J., 1997, 11: 909.Google Scholar
  15. 15.
    Wu, W., Yen, L. F., Immunochemical identification of gelsolin in maize pollen, Chin. Sci. Bull. (in Chinese), 1997, 42: 1784.Google Scholar
  16. 16.
    Ren, D. T., Liu, A. X., Yen, L. F., Immunochemical identification and immunofluorescent localization of tropomyosin in germinated pollen ofLilium davidii, Prog in Nat. Sci., 1999, 9: 230.Google Scholar
  17. 17.
    Teng, X. Y., Wang, X. Z., Yen, L. F., Cytoplasmic male sterility and actin in pollens, J. Beijing Agri. Univ. (in Chinese), 1986, 12(1): 15.Google Scholar
  18. 18.
    Shah, D. M., Hightower, R. C., Meagher, R. B., Complete nucleotide sequence of soybean actin gene, Proc. Natl. Acad. Sci. USA, 1982, 79: 1022.PubMedCrossRefGoogle Scholar
  19. 19.
    Reece, K. S., McElroy, D., Wu, R. et al., Genomic nucleatide sequence of four rice (Oryza sative) actin genes, Plant Mol. Biol., 1990, 14: 621.PubMedCrossRefGoogle Scholar
  20. 20.
    Cao, X. F., Wang, R. C., Yen, L. F. et al., Construction of a pea tendril cDNA library and sequence analysis of a pea actin cDNA, PEAcl, Chin. Sci. Bull., 1994, 39(4): 332.Google Scholar
  21. 21.
    Kabsch, W., Mannherz, H. G., Suck, D. et al., Atomic structure of the actin: DNase complex, Nature, 1990, 347: 37.PubMedCrossRefGoogle Scholar
  22. 22.
    Mascarenhas, J. P., Characterization of genes that are expressed in pollens, in The Molecular Basis of Plant Development (ed. Goldberg, R. B.), 1989, pp. 90–105.Google Scholar
  23. 23.
    Huang, S. X., Liu, J. J., Yen, L. F. et al., Expression of actin gene during development of snake gourd and cucumber, Acta Bot. Sin. (in Chinese), 1996, 38: 136.Google Scholar
  24. 24.
    Huang, S. X., Liu, J. J., Yen, L. F. et al., Developmental stage and organ-specific expression of actin genes in seedling ofPisum sativum, J. China Agri. Univ. (in Chinese), 1997, 2: 25.Google Scholar
  25. 25.
    Kandasamy, M. K., McKinney, E. C., Meagher, R. B., The late pollen-specific actins in angiosperms, Plant J., 1999, 18(6): 681.PubMedCrossRefGoogle Scholar
  26. 26.
    McElroy, D., Zhang, W., Cao, J. et al., Isolation of an efficient actin promoter for use in rice transformation, Plant Cell, 1990, 2: 163.PubMedCrossRefGoogle Scholar
  27. 27.
    Weintraub, H. M., Antisense RNA and DNA, Scien. Amer., 1990, January: 34.Google Scholar

Copyright information

© Science in China Press 2000

Authors and Affiliations

  1. 1.Laboratory of Plant Physiology and BiochomistryMinistry of AgriultureBeijingChina
  2. 2.College of Biological SciencesChina Agricultural UniversityBeijingChina

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