Abstract
Two highly similar cytosolic Cu/Zn Sod (Sod4 and Sod4A) genes have been isolated from maize. Sod4A contains eight exons and seven introns. The Sod4 partial sequence contains five introns. The introns in both genes are located in the same position and have highly homologous sequences in several regions. The largest intron (>1200 bp) interrupts the 5' leader sequence. The presence of different regulatory motifs in the promoter region of each gene may indicate distinct responses to various conditions. Zymogram and RNA blot analyses show that Sod4 and Sod4A are expressed in all tissues of the maize plant. The developmental profiles of Sod4 and Sod4A mRNA accumulation differ in scutella during sporophytic development. RNA blot analysis of the respective Sod mRNAs indicates a differential, tissue-specific response of each gene to certain stressors. RNA isolated from stem tissue of ethephon-treated seedlings shows an increase in the Sod4 but not the Sod4A transcript while there is no change in transcripts of either gene in leaves or roots. There is differential mRNA accumulation between the two genes in leaf and stem tissue of paraquat-treated seedlings. Other agents that can cause oxidative stress were also tested for differential expression of the genes.
Full Text
The Full Text of this article is available as a PDF (8.4 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Armstrong G. A., Weisshaar B., Hahlbrock K. Homodimeric and heterodimeric leucine zipper proteins and nuclear factors from parsley recognize diverse promoter elements with ACGT cores. Plant Cell. 1992 May;4(5):525–537. doi: 10.1105/tpc.4.5.525. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Bermingham-McDonogh O., Gralla E. B., Valentine J. S. The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4789–4793. doi: 10.1073/pnas.85.13.4789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
- Cannon R. E., White J. A., Scandalios J. G. Cloning of cDNA for maize superoxide dismutase 2 (SOD2). Proc Natl Acad Sci U S A. 1987 Jan;84(1):179–183. doi: 10.1073/pnas.84.1.179. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Conley T. R., Park S. C., Kwon H. B., Peng H. P., Shih M. C. Characterization of cis-acting elements in light regulation of the nuclear gene encoding the A subunit of chloroplast isozymes of glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana. Mol Cell Biol. 1994 Apr;14(4):2525–2533. doi: 10.1128/mcb.14.4.2525. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Farrington J. A., Ebert M., Land E. J., Fletcher K. Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides. Biochim Biophys Acta. 1973 Sep 26;314(3):372–381. doi: 10.1016/0005-2728(73)90121-7. [DOI] [PubMed] [Google Scholar]
- Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
- Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem. 1995;64:97–112. doi: 10.1146/annurev.bi.64.070195.000525. [DOI] [PubMed] [Google Scholar]
- Fridovich I. The biology of oxygen radicals. Science. 1978 Sep 8;201(4359):875–880. doi: 10.1126/science.210504. [DOI] [PubMed] [Google Scholar]
- Giuliano G., Pichersky E., Malik V. S., Timko M. P., Scolnik P. A., Cashmore A. R. An evolutionarily conserved protein binding sequence upstream of a plant light-regulated gene. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7089–7093. doi: 10.1073/pnas.85.19.7089. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Green P. J., Yong M. H., Cuozzo M., Kano-Murakami Y., Silverstein P., Chua N. H. Binding site requirements for pea nuclear protein factor GT-1 correlate with sequences required for light-dependent transcriptional activation of the rbcS-3A gene. EMBO J. 1988 Dec 20;7(13):4035–4044. doi: 10.1002/j.1460-2075.1988.tb03297.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Guiltinan M. J., Marcotte W. R., Jr, Quatrano R. S. A plant leucine zipper protein that recognizes an abscisic acid response element. Science. 1990 Oct 12;250(4978):267–271. doi: 10.1126/science.2145628. [DOI] [PubMed] [Google Scholar]
- Harvey R. P., Robins A. J., Wells J. R. Independently evolving chicken histone H2B genes: identification of a ubiquitous H2B-specific 5' element. Nucleic Acids Res. 1982 Dec 11;10(23):7851–7863. doi: 10.1093/nar/10.23.7851. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kardish N., Magal N., Aviv D., Galun E. The tomato gene for the chloroplastic Cu,Zn superoxide dismutase: regulation of expression imposed in transgenic tobacco plants by a short promoter. Plant Mol Biol. 1994 Aug;25(5):887–897. doi: 10.1007/BF00028883. [DOI] [PubMed] [Google Scholar]
- Kernodle S. P., Cannon R. E., Scandalios J. G. Rapid and simple phage DNA isolation. Biotechniques. 1993 Mar;14(3):360–362. [PubMed] [Google Scholar]
- Kim Y. H., Yoo H. Y., Jung G., Kim J. Y., Rho H. M. Isolation and analysis of the rat genomic sequence encoding Cu/Zn superoxide dismutase. Gene. 1993 Nov 15;133(2):267–271. doi: 10.1016/0378-1119(93)90650-r. [DOI] [PubMed] [Google Scholar]
- Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L., Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y. Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J. 1985 Jan;4(1):77–84. doi: 10.1002/j.1460-2075.1985.tb02320.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marcotte W. R., Jr, Russell S. H., Quatrano R. S. Abscisic acid-responsive sequences from the em gene of wheat. Plant Cell. 1989 Oct;1(10):969–976. doi: 10.1105/tpc.1.10.969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matters G. L., Scandalios J. G. Effect of elevated temperature on catalase and superoxide dismutase during maize development. Differentiation. 1986;30(3):190–196. doi: 10.1111/j.1432-0436.1986.tb00780.x. [DOI] [PubMed] [Google Scholar]
- Matters G. L., Scandalios J. G. Effect of the free radical-generating herbicide paraquat on the expression of the superoxide dismutase (Sod) genes in maize. Biochim Biophys Acta. 1986 Jun 3;882(1):29–38. doi: 10.1016/0304-4165(86)90051-6. [DOI] [PubMed] [Google Scholar]
- McLachlan A. D. Repeated folding pattern in copper-zinc superoxide dismutase. Nature. 1980 May 22;285(5762):267–268. doi: 10.1038/285267a0. [DOI] [PubMed] [Google Scholar]
- Ohme-Takagi M., Shinshi H. Ethylene-inducible DNA binding proteins that interact with an ethylene-responsive element. Plant Cell. 1995 Feb;7(2):173–182. doi: 10.1105/tpc.7.2.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palmer J. D., Logsdon J. M., Jr The recent origins of introns. Curr Opin Genet Dev. 1991 Dec;1(4):470–477. doi: 10.1016/s0959-437x(05)80194-7. [DOI] [PubMed] [Google Scholar]
- Pelham H. R. A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell. 1982 Sep;30(2):517–528. doi: 10.1016/0092-8674(82)90249-5. [DOI] [PubMed] [Google Scholar]
- Perler F., Efstratiadis A., Lomedico P., Gilbert W., Kolodner R., Dodgson J. The evolution of genes: the chicken preproinsulin gene. Cell. 1980 Jun;20(2):555–566. doi: 10.1016/0092-8674(80)90641-8. [DOI] [PubMed] [Google Scholar]
- Rushmore T. H., Morton M. R., Pickett C. B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem. 1991 Jun 25;266(18):11632–11639. [PubMed] [Google Scholar]
- Sakamoto A., Okumura T., Ohsuga H., Tanaka K. Genomic structure of the gene for copper/zinc-superoxide dismutase in rice. FEBS Lett. 1992 Apr 20;301(2):185–189. doi: 10.1016/0014-5793(92)81244-g. [DOI] [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scandalios J. G. Oxygen Stress and Superoxide Dismutases. Plant Physiol. 1993 Jan;101(1):7–12. doi: 10.1104/pp.101.1.7. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seto N. O., Hayashi S., Tener G. M. The sequence of the Cu-Zn superoxide dismutase gene of Drosophila. Nucleic Acids Res. 1987 Dec 23;15(24):10601–10601. doi: 10.1093/nar/15.24.10601. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sorger P. K. Heat shock factor and the heat shock response. Cell. 1991 May 3;65(3):363–366. doi: 10.1016/0092-8674(91)90452-5. [DOI] [PubMed] [Google Scholar]
- 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]
- Wolffe A. P. Structural and functional properties of the evolutionarily ancient Y-box family of nucleic acid binding proteins. Bioessays. 1994 Apr;16(4):245–251. doi: 10.1002/bies.950160407. [DOI] [PubMed] [Google Scholar]
- 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]