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Superoxide Dismutase in Arabidopsis: An Eclectic Enzyme Family
with Disparate Regulation and Protein Localization1
Daniel J. Kliebenstein,
Rita-Ann Monde, and
Robert L. Last2, *
Boyce Thompson Institute for Plant Research, and Section of
Genetics and Development (D.J.K., R.L.L.), and Section of Biochemistry,
Molecular and Cellular Biology (R.-A.M.), Cornell University, Tower
Road, Ithaca, New York 14853-1801
A
number of environmental stresses can lead to enhanced production of
superoxide within plant tissues, and plants are believed to rely on the
enzyme superoxide dismutase (SOD) to detoxify this reactive oxygen
species. We have identified seven cDNAs and genes for SOD in
Arabidopsis. These consist of three CuZnSODs (CSD1, CSD2, and CSD3), three FeSODs
(FSD1, FSD2, and FSD3),
and one MnSOD (MSD1). The chromosomal location of these
seven SOD genes has been established. To study this enzyme family,
antibodies were generated against five proteins: CSD1, CSD2, CSD3,
FSD1, and MSD1. Using these antisera and nondenaturing-polyacrylamide gel electrophoresis enzyme assays, we identified protein and activity for two CuZnSODs and for FeSOD and MnSOD in Arabidopsis rosette tissue.
Additionally, subcellular fractionation studies revealed the presence
of CSD2 and FeSOD protein within Arabidopsis chloroplasts. The seven
SOD mRNAs and the four proteins identified were differentially regulated in response to various light regimes, ozone fumigation, and
ultraviolet-B irradiation. To our knowledge, this is the first report
of a large-scale analysis of the regulation of multiple SOD proteins in
a plant species.
1
This work was supported by grant no.
96-35100-3212 from the Plant Responses to the Envrionment Program of
the National Research Initiative Competitive Grants Program, U.S.
Department of Agriculture. D.J.K. received support from a National
Institutes of Health predoctoral training grant fellowship through the
Section of Genetics and Development, Cornell University.
2
Present address: Cereon Genomics, 1 Kendall
Square, Building 300, Cambridge, MA 02139.
*
Corresponding author; e-mail rob.last{at}cereon.com; fax
1-607-255-6695.
Plant Physiol. (1998) 118: 637-650
Copyright Clearance Center: 0032-0889/98/118//14
© 1998 American Society of Plant Physiologists
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