Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1994 Sep;106(1):173–178. doi: 10.1104/pp.106.1.173

Differential Accumulation of Manganese-Superoxide Dismutase Transcripts in Maize in Response to Abscisic Acid and High Osmoticum.

D Zhu 1, J G Scandalios 1
PMCID: PMC159513  PMID: 12232316

Abstract

The plant growth regulator abscisic acid (ABA) has multiple physiological effects during embryogenesis and seed formation. Although a number of genes induced by ABA have been characterized, the functions of the encoded proteins remain, for the most part, obscure. In this paper we demonstrate that members of the manganese-superoxide dismutase (MnSod) gene family encoding antioxidant isozymes of known function during development and oxidative stress respond differentially to ABA and high osmoticum in developing maize (Zea mays L.) embryos. Expression of the maize Sod3.1 does not respond to ABA or high osmoticum, whereas the steady-state levels of the maize Sod3.2, Sod3.3, and Sod3.4 transcripts are induced by ABA. Total SOD-3 protein and enzymatic activity, however, remain constant. Additionally, we examined the requirement for ABA in the accumulation of MnSod transcripts in response to high osmoticum in wild-type and mutant embryos of an ABA-deficient line (M1A4; vp5). RNA blot analyses show that multiple Sod3 transcripts are also found in line M1A4, and ABA increases the accumulation of the Sod3.2, Sod3.3, and Sod3.4 transcripts in both wild-type and vp5 mutant embryos. Interestingly, although accumulation of the Sod3.3 and Sod3.4 transcripts in the vp5 mutant embryo was induced by ABA, it was not induced by high osmoticum. Both superoxide dismutase and ABA have been implicated in plant tolerance to environmental stress; results from this study demonstrate a connection between the action of ABA and oxidative stress during embryo maturation in maize.

Full Text

The Full Text of this article is available as a PDF (1.6 MB).

Selected References

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

  1. Baum J. A., Scandalios J. G. Isolation and characterization of the cytosolic and mitochondrial superoxide dismutases of maize. Arch Biochem Biophys. 1981 Feb;206(2):249–264. doi: 10.1016/0003-9861(81)90089-8. [DOI] [PubMed] [Google Scholar]
  2. Beachy R. N., Chen Z. L., Horsch R. B., Rogers S. G., Hoffmann N. J., Fraley R. T. Accumulation and assembly of soybean beta-conglycinin in seeds of transformed petunia plants. EMBO J. 1985 Dec 1;4(12):3047–3053. doi: 10.1002/j.1460-2075.1985.tb04044.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bowler C., Alliotte T., De Loose M., Van Montagu M., Inzé D. The induction of manganese superoxide dismutase in response to stress in Nicotiana plumbaginifolia. EMBO J. 1989 Jan;8(1):31–38. doi: 10.1002/j.1460-2075.1989.tb03345.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bowler C., Slooten L., Vandenbranden S., De Rycke R., Botterman J., Sybesma C., Van Montagu M., Inzé D. Manganese superoxide dismutase can reduce cellular damage mediated by oxygen radicals in transgenic plants. EMBO J. 1991 Jul;10(7):1723–1732. doi: 10.1002/j.1460-2075.1991.tb07696.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cannon R. E., Scandalios J. G. Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase proteins in maize. Mol Gen Genet. 1989 Oct;219(1-2):1–8. doi: 10.1007/BF00261150. [DOI] [PubMed] [Google Scholar]
  6. Chen Z., Silva H., Klessig D. F. Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid. Science. 1993 Dec 17;262(5141):1883–1886. doi: 10.1126/science.8266079. [DOI] [PubMed] [Google Scholar]
  7. Delisle A. J., Crouch M. L. Seed Storage Protein Transcription and mRNA Levels in Brassica napus during Development and in Response to Exogenous Abscisic Acid. Plant Physiol. 1989 Oct;91(2):617–623. doi: 10.1104/pp.91.2.617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Devary Y., Gottlieb R. A., Lau L. F., Karin M. Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol. 1991 May;11(5):2804–2811. doi: 10.1128/mcb.11.5.2804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Galau G. A., Bijaisoradat N., Hughes D. W. Accumulation kinetics of cotton late embryogenesis-abundant mRNAs and storage protein mRNAs: coordinate regulation during embryogenesis and the role of abscisic acid. Dev Biol. 1987 Sep;123(1):198–212. doi: 10.1016/0012-1606(87)90442-8. [DOI] [PubMed] [Google Scholar]
  10. Gupta A. S., Heinen J. L., Holaday A. S., Burke J. J., Allen R. D. Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1629–1633. doi: 10.1073/pnas.90.4.1629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hérouart D., Van Montagu M., Inzé D. Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):3108–3112. doi: 10.1073/pnas.90.7.3108. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mihm S., Ennen J., Pessara U., Kurth R., Dröge W. Inhibition of HIV-1 replication and NF-kappa B activity by cysteine and cysteine derivatives. AIDS. 1991 May;5(5):497–503. doi: 10.1097/00002030-199105000-00004. [DOI] [PubMed] [Google Scholar]
  13. Mundy J., Chua N. H. Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. 1988 Aug;7(8):2279–2286. doi: 10.1002/j.1460-2075.1988.tb03070.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Schreck R., Rieber P., Baeuerle P. A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 1991 Aug;10(8):2247–2258. doi: 10.1002/j.1460-2075.1991.tb07761.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Silva C. M., Cidlowski J. A. Direct evidence for intra- and intermolecular disulfide bond formation in the human glucocorticoid receptor. Inhibition of DNA binding and identification of a new receptor-associated protein. J Biol Chem. 1989 Apr 25;264(12):6638–6647. [PubMed] [Google Scholar]
  16. Skriver K., Mundy J. Gene expression in response to abscisic acid and osmotic stress. Plant Cell. 1990 Jun;2(6):503–512. doi: 10.1105/tpc.2.6.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. White J. A., Scandalios J. G. Isolation and characterization of a cDNA for mitochondrial manganese superoxide dismutase (SOD-3) of maize and its relation to other manganese superoxide dismutases. Biochim Biophys Acta. 1988 Nov 10;951(1):61–70. doi: 10.1016/0167-4781(88)90025-5. [DOI] [PubMed] [Google Scholar]
  18. Williamson J. D., Scandalios J. G. Differential response of maize catalases and superoxide dismutases to the photoactivated fungal toxin cercosporin. Plant J. 1992 May;2(3):351–358. doi: 10.1111/j.1365-313x.1992.00351.x. [DOI] [PubMed] [Google Scholar]
  19. Xanthoudakis S., Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J. 1992 Feb;11(2):653–665. doi: 10.1002/j.1460-2075.1992.tb05097.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Xanthoudakis S., Miao G., Wang F., Pan Y. C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 1992 Sep;11(9):3323–3335. doi: 10.1002/j.1460-2075.1992.tb05411.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zhu D., Scandalios J. G. Expression of the maize MnSod (Sod3) gene in MnSOD-deficient yeast rescues the mutant yeast under oxidative stress. Genetics. 1992 Aug;131(4):803–809. doi: 10.1093/genetics/131.4.803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zhu D., Scandalios J. G. Maize mitochondrial manganese superoxide dismutases are encoded by a differentially expressed multigene family. Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9310–9314. doi: 10.1073/pnas.90.20.9310. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES