Copper deficiency induced expression of Fe-superoxide dismutase gene in Matteuccia struthiopteris

Plant Physiology and Biochemistry

Volumn 42, Issue 2, 2004, Pages 143-148

  Murao, Kenichi ^a   Takamiya, Masayuki ^a   Ono, Kanji ^a   Takano, Hiroyoshi ^a   Takio, Susumu ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Copper deficiency; Fe superoxide dismutase; Fern; Matteuccia struthiopteris

Indexed keywords

EQUISETUM; EQUISETUM ARVENSE; ESCHERICHIA COLI; FILICOPHYTA; MATTEUCCIA STRUTHIOPTERIS;

EID: 1242344063     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2003.11.004     Document Type: Article

References (27)

1. Amasino R.M., Crowell D.N. Nucleotide sequence of an iron superoxide dismutase complementary DNA from soybean. Plant Physiol. 96:1991;1393-1394.
2. Ayala M.B., Sandmann G. Activities of Cu-containing protein in Cu-depleted pea leaves. Physiol. Plant. 72:1988;801-806.
3. Beauchamp C.O., Fridovich I. Superoxide dismutase improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:1971;276-287.
4. Beyer W.F., Fridovich I. Assaying for superoxide dismutase activity: some large consequence of minor change in conditions. Anal. Biochem. 72:1976;248-254.
5. Bowler C., Van Camp W., Van Montagu M., Inzé D. Superoxide dismutase in plants. CRC Crit. Rev. Plant Sci. 13:1994;199-218.
6. Bowler C., Van Montagu M., Inzé D. Superoxide dismutase and stress tolerance. Annu. Rev. Plant Physiol. Plant Mol. Biol. 43:1992;83-116.
7. 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. 72:1976;248-254.
8. Bridges S.M., Salin M.L. Distribution of iron-containing superoxide dismutase in vascular plants. Plant Physiol. 68:1981;275-278.
9. Chen H.-Y., Hu R.-G., Wang B.-Z., Chen W.-F., Liu W.-Y., Schröder W., Frank P., Ulbrich N. Structural studies of an eukaryotic cambialistic superoxide dismutase purified from the mature seeds of camphor tree. Arch. Biochem. Biophys. 404:2002;218-226.
10. Cortez N., Carrillo N., Pasternak C., Balzer A., Klug G. Molecular cloning and expression analysis of the Rhodobacter capsulatus sodB gene, encoding an iron superoxide dismutase. J. Bacteriol. 180:1998;5413-5420.
11. Kaminaka H., Morita S., Tokumoto M., Yokoyama H., Masumura T., Tanaka K. Molecular cloning and characterization of a cDNA for an iron-superoxide dismutase in rice (Oryza sativa L.). Biosci. Biotechnol. Biochem. 63:1999;302-308.
12. Kanematsu S., Asada K. Superoxide dismutase. Fukui T., Soda K. Molecular Aspects of Enzyme Catalysis. 1994;191-210 Kodansya, Tokyo.
13. Kliebenstein D.J., Monde R.A., Last R.L. Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization. Plant Physiol. 118:1998;637-650.
14. Kurepa J., Van Montagu M. D. Inzé, Expression of sodCp and sodB genes in Nicotiana tabacum: effects of light copper excess. J. Exp. Bot. 48:1997;2007-2014.
15. Kwiatowski J., Safianowska A., Kaniuga Z. Isolation and characterization of an iron-containing superoxide dismutase from tomato leaves, Lycopersicon esculentum. Eur. J. Biochem. 146:1985;459-466.
16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
17. Martin M.E., Byers B.R., Olson M.O., Salin M.L., Arceneaux J.E., Tolbert C. A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor. J. Biol. Chem. 261:1986;9361-9367.
18. Murashige T., Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15:1962;473-497.
19. Sakamoto A., Nosaka Y., Tanaka K. Cloning and sequencing analysis of a complementary DNA for manganese-superoxide dismutase from rice (Oryza sativa L.). Plant Physiol. 103:1993;1477-1478.
20. Salin M.L., Bridges S.M. Absence of the iron-containing superoxide dismutase in mitochondria from mustard (Brassica campestris). Biochem. J. 195:1981;229-233.
21. Santos R., Bocquet S., Puppo A., Touati D. Characterization of an atypical superoxide dismutase from Sinorhizobium meliloti. J. Bacteriol. 181:1999;4509-4516.
22. Shiono T., Nakata M., Yamahara T., Matsuzaki M., Deguchi H., Satoh T. Repression by Cu of the expression of Fe-superoxide dismutase of chloroplasts in the moss Barbula unguiculata but not in the liverwort Marchantia paleacea var. diptera. J. Hattori Bot. Lab. 93:2003;141-153.
23. Suzuki T., Takio S., Satoh T. Light-dependent expression in liverwort cells of chlL/N and chlB identified as chloroplast genes involved in chlorophyll synthesis in the dark. J. Plant Physiol. 152:1998;31-37.
24. Tabares L.C., Bittel C., Carrillo N., Bortolotti A., Cortez N. The single superoxide dismutase of Rhodobacter capsulatus is a cambialistic, manganese-containing enzyme. J. Bacteriol. 185:2003;3223-3227.
25. Van Camp W., Bowler C., Villarroel R., Tsang E.W.T., Van Montagu M.M., Inzé D. Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Proc. Natl. Acad. Sci. USA. 87:1990;9903-9907.
26. Wong-Vega L., Burke J.J., Allen R.D. Isolation and sequence analysis of a cDNA that encodes pea manganese superoxide dismutase. Plant Mol. Biol. 17:1991;1271-1274.
27. Zhu D., Scandalios J.G. Maize mitochondrial manganese superoxide dismutase are encoded by a differentially expressed multigene family. Proc. Natl. Acad. Sci. USA. 90:1993;9310-9314.