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. 1993 Jan;101(1):193–199. doi: 10.1104/pp.101.1.193

Identification of a basic glycoprotein induced by ethylene in primary leaves of azuki bean as a cationic peroxidase.

F Ishige 1, H Mori 1, K Yamazaki 1, H Imaseki 1
PMCID: PMC158664  PMID: 8278494

Abstract

Ethylene causes the accumulation of seven different proteins (each designated AZxx according to its molecular mass, xx in kD) in excised primary leaves of azuki bean (Vigna angularis) (F. Ishige, H. Mori, K. Yamazaki, H. Imaseki [1991] Plant Cell Physiol 32: 681-690). A complementary DNA encoding an ethylene-induced basic glycoprotein, AZ42, from azuki bean was cloned and its complete nucleotide sequence was determined. Characterization of the cDNA was accomplished by monitoring expression of an immunoreactive protein in Escherichia coli that harbored the cDNA and by the identification of a partial amino acid sequence that was the same as that determined from the purified protein. An open reading frame (1071 base pairs) in the cDNA encoded a protein of 357 amino acids with a molecular mass of 39.3 kD. The amino acid sequence contained three regions that are highly conserved among peroxidases from eight different plants. Purified AZ42 exhibited peroxidase activity. The basic glycoprotein induced by ethylene was identified as a cationic isozyme of peroxidase. The corresponding mRNA was not present in leaves that had not been treated with ethylene, but it appeared after 1 h of treatment with ethylene and its level increased for the next 15 h. Accumulation of the mRNA was also induced after wounding or treatment with salicylate. The wound-induced increase in the level of the mRNA was suppressed by 2,5-norbornadiene, but the salicylate-induced increase was not.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Broglie K. E., Gaynor J. J., Broglie R. M. Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6820–6824. doi: 10.1073/pnas.83.18.6820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Buffard D., Breda C., van Huystee R. B., Asemota O., Pierre M., Ha D. B., Esnault R. Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8874–8878. doi: 10.1073/pnas.87.22.8874. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ecker J. R., Davis R. W. Plant defense genes are regulated by ethylene. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5202–5206. doi: 10.1073/pnas.84.15.5202. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J. K., Shinmyo A., Takano M., Yamada Y., Okada H. Structure of the horseradish peroxidase isozyme C genes. Eur J Biochem. 1988 May 2;173(3):681–687. doi: 10.1111/j.1432-1033.1988.tb14052.x. [DOI] [PubMed] [Google Scholar]
  6. Lagrimini L. M., Burkhart W., Moyer M., Rothstein S. Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7542–7546. doi: 10.1073/pnas.84.21.7542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lagrimini L. M., Rothstein S. Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection. Plant Physiol. 1987 Jun;84(2):438–442. doi: 10.1104/pp.84.2.438. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Lincoln J. E., Cordes S., Read E., Fischer R. L. Regulation of gene expression by ethylene during Lycopersicon esculentum (tomato) fruit development. Proc Natl Acad Sci U S A. 1987 May;84(9):2793–2797. doi: 10.1073/pnas.84.9.2793. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Malamy J., Carr J. P., Klessig D. F., Raskin I. Salicylic Acid: a likely endogenous signal in the resistance response of tobacco to viral infection. Science. 1990 Nov 16;250(4983):1002–1004. doi: 10.1126/science.250.4983.1002. [DOI] [PubMed] [Google Scholar]
  10. Rasmussen S. K., Welinder K. G., Hejgaard J. cDNA cloning, characterization and expression of an endosperm-specific barley peroxidase. Plant Mol Biol. 1991 Feb;16(2):317–327. doi: 10.1007/BF00020562. [DOI] [PubMed] [Google Scholar]
  11. Roberts E., Kolattukudy P. E. Molecular cloning, nucleotide sequence, and abscisic acid induction of a suberization-associated highly anionic peroxidase. Mol Gen Genet. 1989 Jun;217(2-3):223–232. doi: 10.1007/BF02464885. [DOI] [PubMed] [Google Scholar]
  12. Rocha-Sosa M., Sonnewald U., Frommer W., Stratmann M., Schell J., Willmitzer L. Both developmental and metabolic signals activate the promoter of a class I patatin gene. EMBO J. 1989 Jan;8(1):23–29. doi: 10.1002/j.1460-2075.1989.tb03344.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Welinder K. G. Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase. Eur J Biochem. 1985 Sep 16;151(3):497–504. doi: 10.1111/j.1432-1033.1985.tb09129.x. [DOI] [PubMed] [Google Scholar]

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