메뉴 건너뛰기




Volumn 63, Issue 2, 1999, Pages 302-308

Molecular cloning and characterization of a cdna for an iron-superoxide dismutase in rice (oryza sativa l.)

Author keywords

Active oxygen; Cdna cloning; Gene expression; Iron superoxide dismutase (EC 1.15.1.1); Rice (Oryza sativa L. cv Nipponbare)

Indexed keywords

DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; IRON; MANGANESE; NITROBLUE TETRAZOLIUM; PLANT DNA; RECOMBINANT PROTEIN; SUPEROXIDE DISMUTASE;

EID: 0033069393     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.302     Document Type: Article
Times cited : (44)

References (29)
  • 1
    • 0022480378 scopus 로고
    • Superoxide dismutases
    • Fridovich, I., Superoxide dismutases. Adv. Enzymol., 58, 61-97 (1986).
    • (1986) Adv. Enzymol. , vol.58 , pp. 61-97
    • Fridovich, I.1
  • 3
    • 0021126946 scopus 로고
    • Manganese and iron super oxide dismutases are structural homologs.J
    • Stallings, W. C., Pattridge, K. A., Strong, R. K., and Ludwig, M. L., Manganese and iron super oxide dismutases are structural homologs.J. Biol. Chem., 259, 10695-10699 (1984).
    • (1984) Biol. Chem. , vol.259 , pp. 10695-10699
    • Stallings, W.C.1    Pattridge, K.A.2    Strong, R.K.3    Ludwig, M.L.4
  • 4
    • 0025686977 scopus 로고
    • Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli
    • Van Camp, W., Bowler, C., Villarroel, R., Tsang, E. W. T., Montagu, M. V., and Inze, D., Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Proc. Natl. Acad. Sci. USA, 87, 9903-9907 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9903-9907
    • Van Camp, W.1    Bowler, C.2    Villarroel, R.3    Tsang, E.W.T.4    Montagu, M.V.5    Inze, D.6
  • 5
    • 0001620959 scopus 로고
    • Distribution of iron-containing superoxide dismutase in vascular plants
    • Briges, S. M. and Salin, M. L., Distribution of iron-containing superoxide dismutase in vascular plants. Plant Physiol., 68, 275-278 (1981).
    • (1981) Plant Physiol. , vol.68 , pp. 275-278
    • Briges, S.M.1    Salin, M.L.2
  • 6
    • 0019012141 scopus 로고
    • Isolation and characterization of an iron-containing superoxide dismutase from a eucaryote, Brassica campestris
    • Salin, M. L. and Bridges, S. M., Isolation and characterization of an iron-containing superoxide dismutase from a eucaryote, Brassica campestris. Arch. Biochem. Biophys., 201, 369-374 (1980).
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 369-374
    • Salin, M.L.1    Bridges, S.M.2
  • 7
    • 0022425323 scopus 로고
    • Isolation and characterization of an iron-containing superoxide dismutase from tomato leaves, Lycopersicon esculentum
    • Kwiatowski, J., Safianowska, A., and Kaniuga, Z., Isolation and characterization of an iron-containing superoxide dismutase from tomato leaves, Lycopersicon esculentum. Eur. J. Biochem., 146, 459-466 (1985).
    • (1985) Eur. J. Biochem. , vol.146 , pp. 459-466
    • Kwiatowski, J.1    Safianowska, A.2    Kaniuga, Z.3
  • 8
    • 0025930291 scopus 로고
    • L. A. and Sevilla, F. Purification of an iron-containing superoxide dismutase from a citrus plant, Citrus limonum R
    • Almansa, M. S., Palma, J. M., Yanez, J., del Rio., L. A., and Sevilla, F., Purification of an iron-containing superoxide dismutase from a citrus plant, Citrus limonum R. Free Radic. Res. Commun., 12, 319-328 (1991).
    • (1991) Free Radic. Res. Commun. , vol.12 , pp. 319-328
    • Almansa, M.S.1    Palma, J.M.2    Yanez, J.3    Del, R.4
  • 9
    • 0002879408 scopus 로고
    • CuZn-superoxide dismutase in rice: Occurrence of an active, monomeric enzyme and two types of isozyme in leaf and non-photosynthetic tissues
    • Kanematsu, S. and Asada, K., CuZn-superoxide dismutase in rice: occurrence of an active, monomeric enzyme and two types of isozyme in leaf and non-photosynthetic tissues. Plant Cell Physiol., 30, 381-391 (1989).
    • (1989) Plant Cell Physiol. , vol.30 , pp. 381-391
    • Kanematsu, S.1    Asada, K.2
  • 10
    • 0026863931 scopus 로고
    • Nucleotide sequences of two cDNA clones encoding different Cu/Zn-su-peroxide dismutases expressed in developing rice seed (Oryza sati-va L.)
    • Sakamoto, A., Ohsuga, H., and Tanaka, K., Nucleotide sequences of two cDNA clones encoding different Cu/Zn-su-peroxide dismutases expressed in developing rice seed (Oryza sati-va L.). Plant Mol. Biol., 19, 323-327 (1992).
    • (1992) Plant Mol. Biol. , vol.19 , pp. 323-327
    • Sakamoto, A.1    Ohsuga, H.2    Tanaka, K.3
  • 11
    • 0031002633 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA for plastidic copper/zinc-superoxide dismutase in rice (Oryza sativa L.)
    • Kaminaka H., Morita, S., Yokoi, H., Masumura, T., and Tanaka, K., Molecular cloning and characterization of a cDNA for plastidic copper/zinc-superoxide dismutase in rice (Oryza sativa L.). Plant Cell Physiol., 38, 65-69 (1997).
    • (1997) Plant Cell Physiol. , vol.38 , pp. 65-69
    • Kaminaka, H.1    Morita, S.2    Yokoi, H.3    Masumura, T.4    Tanaka, K.5
  • 12
    • 0027762219 scopus 로고
    • Cloning and sequencing analysis of a complementary DNA for manganese-su-peroxide dismutase from rice (Oryza sativa L.)
    • Sakamoto, A., Nosaka, Y., and Tanaka, K., Cloning and sequencing analysis of a complementary DNA for manganese-su-peroxide dismutase from rice (Oryza sativa L.). Plant Physiol., 103, 1477-1478 (1993).
    • (1993) Plant Physiol. , vol.103 , pp. 1477-1478
    • Sakamoto, A.1    Nosaka, Y.2    Tanaka, K.3
  • 15
    • 0028924856 scopus 로고
    • Structure and differential response to abscisic acid of two promoters for the cytosolic copper /zinc-superoxide dismutase genes, SodCcl and SodCc2, in rice protoplasts
    • Sakamoto, A., Okumura, T., Kaminaka, H., Sumi, K., and Tanaka, K., Structure and differential response to abscisic acid of two promoters for the cytosolic copper /zinc-superoxide dismutase genes, SodCcl and SodCc2, in rice protoplasts. FEBS Lett., 358, 62-66 (1995).
    • (1995) FEBS Lett. , vol.358 , pp. 62-66
    • Sakamoto, A.1    Okumura, T.2    Kaminaka, H.3    Sumi, K.4    Tanaka, K.5
  • 16
    • 0028801607 scopus 로고
    • Changes in organelle superoxide dismutase isoenzymes during air adaptation of submerged rice seedlings: Differential behaviour of isoenzymes in plastids and mitochondria
    • Ushimaru, T., Ogawa, K., Ishida, N., Shibasaka, M., Kanematsu, S., Asada, K., and Tsuji, H., Changes in organelle superoxide dismutase isoenzymes during air adaptation of submerged rice seedlings: differential behaviour of isoenzymes in plastids and mitochondria. Planta, 196, 606-613 (1995).
    • (1995) Planta , vol.196 , pp. 606-613
    • Ushimaru, T.1    Ogawa, K.2    Ishida, N.3    Shibasaka, M.4    Kanematsu, S.5    Asada, K.6    Tsuji, H.7
  • 17
    • 0028192044 scopus 로고
    • Sensitivity of superoxide dismutase transcript levels and activities to oxidative stress is lower in mature-senescent than in young barley leaves
    • Casano, L. M., Martin, M., and Sabater, B., Sensitivity of superoxide dismutase transcript levels and activities to oxidative stress is lower in mature-senescent than in young barley leaves. Plant Physiol., 106, 1033-1039 (1994).
    • (1994) Plant Physiol. , vol.106 , pp. 1033-1039
    • Casano, L.M.1    Martin, M.2    Sabater, B.3
  • 18
    • 0000079458 scopus 로고
    • Nucleotide sequence of an iron superoxide dismutase complementary DNA from soybean
    • Crowell, D. N. and Amasino, R. M., Nucleotide sequence of an iron superoxide dismutase complementary DNA from soybean. Plant Physiol., 96, 1393-1394 (1991).
    • (1991) Plant Physiol. , vol.96 , pp. 1393-1394
    • Crowell, D.N.1    Amasino, R.M.2
  • 19
    • 0015903497 scopus 로고
    • An iron-containing superoxide dis-mutase from Escherichia coli
    • Yost, F. J. and Fridovich, I., An iron-containing superoxide dis-mutase from Escherichia coli. J. Biol. Chem., 248, 4905-4908 (1973)
    • (1973) J. Biol. Chem. , vol.248 , pp. 4905-4908
    • Yost, F.J.1    Fridovich, I.2
  • 20
    • 0014962945 scopus 로고
    • Superoxide dis-mutase from Escherichia coli B. A new manganese-containing enzyme
    • Keel, B. B., McCord, J. M., and Fridovuch, I., Superoxide dis-mutase from Escherichia coli B. A new manganese-containing enzyme. J. Biol. Chem., 245, 6176-6181 (1970)
    • (1970) J. Biol. Chem. , vol.245 , pp. 6176-6181
    • Keel, B.B.1    Mc Cord, J.M.2    Fridovuch, I.3
  • 21
    • 0023130150 scopus 로고
    • Assaying for superoxide dis-mutase activity: Some large consequences of minor changes in conditions
    • Beyer, W. F. and Fridovich I., Assaying for superoxide dis-mutase activity: some large consequences of minor changes in conditions. Anal. Biochem., 161, 559-566 (1987).
    • (1987) Anal. Biochem. , vol.161 , pp. 559-566
    • Beyer, W.F.1    Fridovich, I.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0023945399 scopus 로고
    • Iron- and manganese- containing superoxide dismutases can be distinguished by analysis of their primary structures
    • Parker, M. W. and Blake, C. C. F., Iron- and manganese- containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett., 339, 377-382 (1988).
    • (1988) FEBS Lett. , vol.339 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.F.2
  • 24
    • 0000337179 scopus 로고
    • Induction of specific mR-NAs in cultured soybean cells during cytokinin or auxin starvation
    • Crowell, D. N. and Amasino, R. M., Induction of specific mR-NAs in cultured soybean cells during cytokinin or auxin starvation. Plant Physiol, 95, 711-715 (1991).
    • (1991) Plant Physiol , vol.95 , pp. 711-715
    • Crowell, D.N.1    Amasino, R.M.2
  • 25
    • 0021774481 scopus 로고
    • Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase
    • Yamakura, F., Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase. Biochem. Biophys. Res. Commun., 122, 635-641 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 635-641
    • Yamakura, F.1
  • 26
    • 0000885796 scopus 로고
    • Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts
    • Hayakawa, T., Kanematsu, S., and Asada, K., Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts. Planta, 166, 111-116 (1985).
    • (1985) Planta , vol.166 , pp. 111-116
    • Hayakawa, T.1    Kanematsu, S.2    Asada, K.3
  • 27
    • 0031111135 scopus 로고    scopus 로고
    • Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments
    • Kurepa, J., Herouart, D., Van Montagu, M., and Inze, D., Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments. Plant Cell Physiol., 38, 463-470 (1997).
    • (1997) Plant Cell Physiol. , vol.38 , pp. 463-470
    • Kurepa, J.1    Herouart, D.2    Van Montagu, M.3    Inze, D.4
  • 29
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • Van Camp, W., Capiau, k., Van Montagu, M., Inze, D., and Slooten, L., Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts. Plant Physiol., 112, 1703-1714 (1996).
    • (1996) Plant Physiol. , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiau, K.2    Van Montagu, M.3    Inze, D.4    Slooten, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.