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Characteristic Amino Acid Sequences of Chloroplast and Cytosol Isozymes of CuZn-Superoxide Dismutase in Spinach, Rice and Horsetail

Characteristic Amino Acid Sequences of Chloroplast and Cytosol Isozymes of CuZn-Superoxide... Abstract Two isozymes of CuZn-superoxide dismutase (SOD) were purified from spinach. One (CuZn-SOD II) was localized in chloroplasts and had the same properties as the enzyme previously reported [Asada et al. (1973) Eur. J. Biochem. 36: 257–266]. The other isozyme (CuZn-SOD I) was predominantly expressed in seeds and in etiolated seedlings of spinach, but was localized in the cytosol of the leaves as a minor enzyme. The isozymes have similar molecular weights, subunit structures, and metal contents; but their amino acid compositions, absorption spectra, CD spectra and sensitivities to hydrogen peroxide are different. The amino acid sequences of 50 amino-terminal residues of the chloroplast and cytosol isozymes of CuZn-SOD from spinach, rice and horsetail were determined and compared with those of CuZn-SODs from other plants. The sequences can be divided into chloroplast and cytosol types, and characteristic sequences can be identified in accordance with the observations that the two types of CuZn-SOD isozymes from green algae, ferns and angiosperms can be distinguished immunologically from each other. Differences in amino acid sequences among the cytosol enzymes are greater than those among the chloroplast enzymes, indicating that the rate of mutation of the cytosol CuZn-SOD is higher than that of the chloroplast CuZn-SOD. These results provide further evidence that the divergence of the two types of isozyme of CuZn-SOD occurred at a very early stage of its acquisition, and that each type of CuZn-SOD has evolved independently. This content is only available as a PDF. © 1990. The Japanese Society of Plant Physiologists (JSPP) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant and Cell Physiology Oxford University Press

Characteristic Amino Acid Sequences of Chloroplast and Cytosol Isozymes of CuZn-Superoxide Dismutase in Spinach, Rice and Horsetail

Kanematsu,, Sumio; Asada,, Kozi
Plant and Cell Physiology , Volume 31 (1) – Jan 1, 1990
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Publisher
Oxford University Press
Copyright
© 1990. The Japanese Society of Plant Physiologists (JSPP)
ISSN
0032-0781
eISSN
1471-9053
DOI
10.1093/oxfordjournals.pcp.a077887
Publisher site
See Article on Publisher Site

Abstract

Abstract Two isozymes of CuZn-superoxide dismutase (SOD) were purified from spinach. One (CuZn-SOD II) was localized in chloroplasts and had the same properties as the enzyme previously reported [Asada et al. (1973) Eur. J. Biochem. 36: 257–266]. The other isozyme (CuZn-SOD I) was predominantly expressed in seeds and in etiolated seedlings of spinach, but was localized in the cytosol of the leaves as a minor enzyme. The isozymes have similar molecular weights, subunit structures, and metal contents; but their amino acid compositions, absorption spectra, CD spectra and sensitivities to hydrogen peroxide are different. The amino acid sequences of 50 amino-terminal residues of the chloroplast and cytosol isozymes of CuZn-SOD from spinach, rice and horsetail were determined and compared with those of CuZn-SODs from other plants. The sequences can be divided into chloroplast and cytosol types, and characteristic sequences can be identified in accordance with the observations that the two types of CuZn-SOD isozymes from green algae, ferns and angiosperms can be distinguished immunologically from each other. Differences in amino acid sequences among the cytosol enzymes are greater than those among the chloroplast enzymes, indicating that the rate of mutation of the cytosol CuZn-SOD is higher than that of the chloroplast CuZn-SOD. These results provide further evidence that the divergence of the two types of isozyme of CuZn-SOD occurred at a very early stage of its acquisition, and that each type of CuZn-SOD has evolved independently. This content is only available as a PDF. © 1990. The Japanese Society of Plant Physiologists (JSPP)

Journal

Plant and Cell Physiology – Oxford University Press

Published: Jan 1, 1990

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