Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1994 Dec;106(4):1471–1481. doi: 10.1104/pp.106.4.1471

Characterization and expression of an antifungal zeamatin-like protein (Zlp) gene from Zea mays.

D E Malehorn 1, J R Borgmeyer 1, C E Smith 1, D M Shah 1
PMCID: PMC159687  PMID: 7846159

Abstract

A cDNA clone encoding a basic thaumatin-like protein of Zea mays was recovered from a mid-development seed cDNA library. The gene, Zlp, encoded a protein that was nearly identical with maize zeamatin and alpha-amylase/trypsin inhibitor. Expression of Zlp mRNA was highest in the endosperm tissue of seed 4 weeks after pollination. Expression of zeamatin-like (ZLP) protein correlated with mRNA; also, a low basal level of ZLP expression in leaf was not appreciably induced by abiotic stresses. ZLP was expressed with its own signal peptide in insect cells and in transgenic Arabidopsis and tomato plants. ZLP was secreted in all three systems, with correct processing of the signal peptide. ZLP expressed in transgenic tomato was found to be partially subjected to a proteolytic cleavage after residue 180, by an unknown mechanism, to give a "nicked" isoform of ZLP. Purified ZLP from all three sources, as well as purified "nicked" ZLP from tomato, demonstrated fungal inhibition against Candida albicans and Trichoderma reesei, with marginal inhibition observed against Alternaria solani and Neurospora crassa.

Full Text

The Full Text of this article is available as a PDF (3.4 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bednarek S. Y., Wilkins T. A., Dombrowski J. E., Raikhel N. V. A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell. 1990 Dec;2(12):1145–1155. doi: 10.1105/tpc.2.12.1145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  3. Brederode F. T., Linthorst H. J., Bol J. F. Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding. Plant Mol Biol. 1991 Dec;17(6):1117–1125. doi: 10.1007/BF00028729. [DOI] [PubMed] [Google Scholar]
  4. Dixon R. A., Harrison M. J. Activation, structure, and organization of genes involved in microbial defense in plants. Adv Genet. 1990;28:165–234. doi: 10.1016/s0065-2660(08)60527-1. [DOI] [PubMed] [Google Scholar]
  5. Edens L., Heslinga L., Klok R., Ledeboer A. M., Maat J., Toonen M. Y., Visser C., Verrips C. T. Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli. Gene. 1982 Apr;18(1):1–12. doi: 10.1016/0378-1119(82)90050-6. [DOI] [PubMed] [Google Scholar]
  6. Hattori M., Sakaki Y. Dideoxy sequencing method using denatured plasmid templates. Anal Biochem. 1986 Feb 1;152(2):232–238. doi: 10.1016/0003-2697(86)90403-3. [DOI] [PubMed] [Google Scholar]
  7. Huynh Q. K., Hironaka C. M., Levine E. B., Smith C. E., Borgmeyer J. R., Shah D. M. Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed. J Biol Chem. 1992 Apr 5;267(10):6635–6640. [PubMed] [Google Scholar]
  8. Kauffmann S., Legrand M., Geoffroy P., Fritig B. Biological function of ;pathogenesis-related' proteins: four PR proteins of tobacco have 1,3-beta-glucanase activity. EMBO J. 1987 Nov;6(11):3209–3212. doi: 10.1002/j.1460-2075.1987.tb02637.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Larosa P. C., Chen Z., Nelson D. E., Singh N. K., Hasegawa P. M., Bressan R. A. Osmotin gene expression is posttranscriptionally regulated. Plant Physiol. 1992 Sep;100(1):409–415. doi: 10.1104/pp.100.1.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Leah R., Tommerup H., Svendsen I., Mundy J. Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J Biol Chem. 1991 Jan 25;266(3):1564–1573. [PubMed] [Google Scholar]
  11. Legrand M., Kauffmann S., Geoffroy P., Fritig B. Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6750–6754. doi: 10.1073/pnas.84.19.6750. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mauch F., Mauch-Mani B., Boller T. Antifungal Hydrolases in Pea Tissue : II. Inhibition of Fungal Growth by Combinations of Chitinase and beta-1,3-Glucanase. Plant Physiol. 1988 Nov;88(3):936–942. doi: 10.1104/pp.88.3.936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Neale A. D., Wahleithner J. A., Lund M., Bonnett H. T., Kelly A., Meeks-Wagner D. R., Peacock W. J., Dennis E. S. Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation. Plant Cell. 1990 Jul;2(7):673–684. doi: 10.1105/tpc.2.7.673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nelson D. E., Raghothama K. G., Singh N. K., Hasegawa P. M., Bressan R. A. Analysis of structure and transcriptional activation of an osmotin gene. Plant Mol Biol. 1992 Jul;19(4):577–588. doi: 10.1007/BF00026784. [DOI] [PubMed] [Google Scholar]
  15. Rebmann G., Mauch F., Dudler R. Sequence of a wheat cDNA encoding a pathogen-induced thaumatin-like protein. Plant Mol Biol. 1991 Aug;17(2):283–285. doi: 10.1007/BF00039506. [DOI] [PubMed] [Google Scholar]
  16. Rodrigo I., Vera P., Frank R., Conejero V. Identification of the viroid-induced tomato pathogenesis-related (PR) protein P23 as the thaumatin-like tomato protein NP24 associated with osmotic stress. Plant Mol Biol. 1991 May;16(5):931–934. doi: 10.1007/BF00015088. [DOI] [PubMed] [Google Scholar]
  17. Shure M., Wessler S., Fedoroff N. Molecular identification and isolation of the Waxy locus in maize. Cell. 1983 Nov;35(1):225–233. doi: 10.1016/0092-8674(83)90225-8. [DOI] [PubMed] [Google Scholar]
  18. Simmons C. R., Litts J. C., Huang N., Rodriguez R. L. Structure of a rice beta-glucanase gene regulated by ethylene, cytokinin, wounding, salicylic acid and fungal elicitors. Plant Mol Biol. 1992 Jan;18(1):33–45. doi: 10.1007/BF00018454. [DOI] [PubMed] [Google Scholar]
  19. Singh N. K., Bracker C. A., Hasegawa P. M., Handa A. K., Buckel S., Hermodson M. A., Pfankoch E., Regnier F. E., Bressan R. A. Characterization of osmotin : a thaumatin-like protein associated with osmotic adaptation in plant cells. Plant Physiol. 1987 Oct;85(2):529–536. doi: 10.1104/pp.85.2.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Uknes S., Mauch-Mani B., Moyer M., Potter S., Williams S., Dincher S., Chandler D., Slusarenko A., Ward E., Ryals J. Acquired resistance in Arabidopsis. Plant Cell. 1992 Jun;4(6):645–656. doi: 10.1105/tpc.4.6.645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  22. Vigers A. J., Roberts W. K., Selitrennikoff C. P. A new family of plant antifungal proteins. Mol Plant Microbe Interact. 1991 Jul-Aug;4(4):315–323. doi: 10.1094/mpmi-4-315. [DOI] [PubMed] [Google Scholar]
  23. Ward E. R., Uknes S. J., Williams S. C., Dincher S. S., Wiederhold D. L., Alexander D. C., Ahl-Goy P., Metraux J. P., Ryals J. A. Coordinate Gene Activity in Response to Agents That Induce Systemic Acquired Resistance. Plant Cell. 1991 Oct;3(10):1085–1094. doi: 10.1105/tpc.3.10.1085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wolf S., Deom C. M., Beachy R., Lucas W. J. Plasmodesmatal function is probed using transgenic tobacco plants that express a virus movement protein. Plant Cell. 1991 Jun;3(6):593–604. doi: 10.1105/tpc.3.6.593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. van Loon L. C., van Kammen A. Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. "Samsun" and "Samsun NN". II. Changes in protein constitution after infection with tobacco mosaic virus. Virology. 1970 Feb;40(2):190–211. doi: 10.1016/0042-6822(70)90395-8. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES