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Volumn 19, Issue 1, 1999, Pages 1-8

The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CARBOXY TERMINAL SEQUENCE; CYTOSOL; FREE RADICAL SCAVENGER; GERMINATION; NUCLEOLUS; PEROXIREDOXIN; PLANT EMBRYOGENESIS; PROTEIN LOCALIZATION; REACTIVE OXYGEN METABOLITE; SEED DEVELOPMENT; SEED DORMANCY;

EID: 0033166877     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00488.x     Document Type: Article
Times cited : (110)

References (35)
  • 1
    • 0028388161 scopus 로고
    • The transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds
    • Aalen, R.B., Opsahl-Ferstad, H.-G., Linnestad, C. and Olsen, O.-A. (1994) The transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds. Plant J. 5, 385-396.
    • (1994) Plant J. , vol.5 , pp. 385-396
    • Aalen, R.B.1    Opsahl-Ferstad, H.-G.2    Linnestad, C.3    Olsen, O.-A.4
  • 2
    • 0000749615 scopus 로고
    • Sequence and characterization of s Lea proteins and their genes from cotton
    • Baker, J., Steele, C. and Dure, L., III (1988) Sequence and characterization of S Lea proteins and their genes from cotton. Plant Mol. Biol. 11, 277-291.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 277-291
    • Baker, J.1    Steele, C.2    Dure L. III3
  • 3
    • 0031420258 scopus 로고    scopus 로고
    • Seed germination and dormancy
    • Bewley, J.D. (1997) Seed germination and dormancy. Plant Cell, 9, 1055-1066.
    • (1997) Plant Cell , vol.9 , pp. 1055-1066
    • Bewley, J.D.1
  • 5
    • 0028287515 scopus 로고
    • Putative nuclear localization signals (NLS) in protein transcription factors
    • Boulikas, T. (1994) Putative nuclear localization signals (NLS) in protein transcription factors. J. Cell. Biochem. 55, 32-58.
    • (1994) J. Cell. Biochem. , vol.55 , pp. 32-58
    • Boulikas, T.1
  • 6
    • 0007564053 scopus 로고
    • Protein body formation in the developing barley endosperm
    • Cameron-Mills, V. and von Wettstein, D. (1980) Protein body formation in the developing barley endosperm. Carlsberg Res. Commun. 45, 577-594.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 577-594
    • Cameron-Mills, V.1    Von Wettstein, D.2
  • 7
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G. and Rhee, S.G. (1994a) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl Acad. Sci. USA, 91, 7017-7021.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 8
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • Chae, H.Z., Uhm, T.B. and Rhee, S.G. (1994b) Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl Acad. Sci. USA, 91, 7022-7026.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 9
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994c) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 10
    • 0028814599 scopus 로고
    • Localization of a nuclear protein (QP47) in embryonic meristems during seed maturation and germination and its distribution among crop plants
    • Chiatante, D., Onelli, E., Patrignani, G. and Scippa, G.S. (1995) Localization of a nuclear protein (QP47) in embryonic meristems during seed maturation and germination and its distribution among crop plants. J. Exp. Bot. 46, 815-821.
    • (1995) J. Exp. Bot. , vol.46 , pp. 815-821
    • Chiatante, D.1    Onelli, E.2    Patrignani, G.3    Scippa, G.S.4
  • 11
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins
    • Close, T.J. (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol. Plant. 97, 795-803.
    • (1996) Physiol. Plant. , vol.97 , pp. 795-803
    • Close, T.J.1
  • 12
    • 0028819211 scopus 로고
    • Environmental and hormonal regulation of barley late-embryogenesis-abundant (Lea) mRNAs is via different signal transduction pathways
    • Espelund, M., De Bedout, J.A., Outlaw, W.H. Jr and Jakobsen, K.S. (1995) Environmental and hormonal regulation of barley late-embryogenesis-abundant (Lea) mRNAs is via different signal transduction pathways. Plant Cell. Environ. 18, 943-949.
    • (1995) Plant Cell. Environ. , vol.18 , pp. 943-949
    • Espelund, M.1    De Bedout, J.A.2    Outlaw W.H., Jr.3    Jakobsen, K.S.4
  • 13
    • 0030903157 scopus 로고    scopus 로고
    • The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene
    • Frank, S., Munz, B. and Werner, S. (1997) The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene, 14, 915-921.
    • (1997) Oncogene , vol.14 , pp. 915-921
    • Frank, S.1    Munz, B.2    Werner, S.3
  • 14
    • 0028388157 scopus 로고
    • The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals
    • Goday, A., Jensen, A.B., Culiáñez-Macià, F.A., Albà, M.M., Figueras, M., Serratosa, J., Torrent, M. and Pagès, M. (1994) The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals. Plant Cell, 6, 351-360.
    • (1994) Plant Cell , vol.6 , pp. 351-360
    • Goday, A.1    Jensen, A.B.2    Culiáñez-Macià, F.A.3    Albà, M.M.4    Figueras, M.5    Serratosa, J.6    Torrent, M.7    Pagès, M.8
  • 15
    • 0028675650 scopus 로고
    • Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants
    • Godoy, J.A., Lunar, R., Torres-Schumann, S., Moreno, J., Rodrigo, R.M. and Pintor-Toro, J.A. (1994) Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants. Plant Mol. Biol. 26, 1921-1934.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1921-1934
    • Godoy, J.A.1    Lunar, R.2    Torres-Schumann, S.3    Moreno, J.4    Rodrigo, R.M.5    Pintor-Toro, J.A.6
  • 16
    • 0032055342 scopus 로고    scopus 로고
    • The expression of a peroxiredoxin antioxidant gene, AtPer1, in Arabidopsis thaliana is seed-specific and related to dormancy
    • Haslekås, C., Stacy, R.A.P., Nygaard, V., Culiáñez-Macià, F.A. and Aalen, R.B. (1998) The expression of a peroxiredoxin antioxidant gene, AtPer1, in Arabidopsis thaliana is seed-specific and related to dormancy. Plant Mol. Biol. 36, 833-845.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 833-845
    • Haslekås, C.1    Stacy, R.A.P.2    Nygaard, V.3    Culiáñez-Macià, F.A.4    Aalen, R.B.5
  • 17
    • 0026586047 scopus 로고
    • The VirD2 protein of A. Tumefaciens contains a C-terminal bipartite nuclear localization signal: Implications for nuclear uptake of DNA in plant cells
    • Howard, E.A., Zupan, J.R., Citovsky, V. and Zambryski, P.C. (1992) The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: implications for nuclear uptake of DNA in plant cells. Cell, 68, 109-118.
    • (1992) Cell , vol.68 , pp. 109-118
    • Howard, E.A.1    Zupan, J.R.2    Citovsky, V.3    Zambryski, P.C.4
  • 18
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defence of DNA against oxidative damage
    • Jacobson, F.S., Morgan, R.W., Christman, M.F. and Ames, B.N. (1989) An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defence of DNA against oxidative damage. J. Biol. Chem. 264, 1488-1496.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4
  • 19
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • Kang, S.W., Baines, I.C. and Rhee, S.G. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273, 6303-6311.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 22
    • 0026194271 scopus 로고
    • The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei
    • van der Krol, A.R. and Chua, N.-H. (1991) The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei. Plant Cell, 3, 667-675.
    • (1991) Plant Cell , vol.3 , pp. 667-675
    • Van Der Krol, A.R.1    Chua, N.-H.2
  • 23
    • 0023120755 scopus 로고
    • A new role for phospholipase A2: Protection of membranes from lipid peroxidation damage
    • van Kuijk, F.J.G.M., Sevanian, A., Handelman, G.J. and Dratz, E.A. (1987) A new role for phospholipase A2: protection of membranes from lipid peroxidation damage. Trends Biochem. Sci. 12, 31-34.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 31-34
    • Van Kuijk, F.J.G.M.1    Sevanian, A.2    Handelman, G.J.3    Dratz, E.A.4
  • 24
    • 84972038130 scopus 로고
    • The mechanisms of desiccation tolerance in developing seeds
    • Leprince, O., Hendry, G.A.F. and McKersie, B.D. (1993) The mechanisms of desiccation tolerance in developing seeds. Seed Sci. Res. 3, 231-246.
    • (1993) Seed Sci. Res. , vol.3 , pp. 231-246
    • Leprince, O.1    Hendry, G.A.F.2    McKersie, B.D.3
  • 25
    • 0027947616 scopus 로고
    • The involvement of respiration in free radical processes during loss of desiccation tolerance in germinating Zea mays L
    • Leprince, O., Atherton, N.M., Deltour, R. and Hendry, G.A.F. (1994) The involvement of respiration in free radical processes during loss of desiccation tolerance in germinating Zea mays L. Plant Physiol. 104, 1333-1339.
    • (1994) Plant Physiol. , vol.104 , pp. 1333-1339
    • Leprince, O.1    Atherton, N.M.2    Deltour, R.3    Hendry, G.A.F.4
  • 26
    • 0031402592 scopus 로고    scopus 로고
    • Genetic and molecular control of seed dormancy
    • Li, B. and Foley, M.E. (1997) Genetic and molecular control of seed dormancy. Trends Plant Sci. 2, 384-389.
    • (1997) Trends Plant Sci. , vol.2 , pp. 384-389
    • Li, B.1    Foley, M.E.2
  • 27
    • 0027259213 scopus 로고
    • Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo
    • Lim, Y.S., Cha, M.-K., Kim, H.K., Uhm, T.B., Park, J.W., Kim, K. and Kim, I.H. (1993) Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem. Biophys. Res. Comm. 192, 273-280.
    • (1993) Biochem. Biophys. Res. Comm. , vol.192 , pp. 273-280
    • Lim, Y.S.1    Cha, M.-K.2    Kim, H.K.3    Uhm, T.B.4    Park, J.W.5    Kim, K.6    Kim, I.H.7
  • 28
    • 0029825193 scopus 로고    scopus 로고
    • A barley (Hordeum vulgare L.) LEA3 protein, HVA1, is abundant in protein storage vacuoles
    • Marttila, S., Tenhola, T. and Mikkonen, A. (1996) A barley (Hordeum vulgare L.) LEA3 protein, HVA1, is abundant in protein storage vacuoles. Planta, 199, 602-611.
    • (1996) Planta , vol.199 , pp. 602-611
    • Marttila, S.1    Tenhola, T.2    Mikkonen, A.3
  • 29
    • 0029886243 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by thiol-specific antioxidant enzymes (TSA) is involved with its antioxidant properties - TSA possesses thiol peroxidase activity
    • Netto, L., Chae, H.Z., Kang, S.W., Rhee, S.G. and Stadtman, E.R. (1996) Removal of hydrogen peroxide by thiol-specific antioxidant enzymes (TSA) is involved with its antioxidant properties - TSA possesses thiol peroxidase activity. J. Biol. Chem. 271, 15315-15321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15315-15321
    • Netto, L.1    Chae, H.Z.2    Kang, S.W.3    Rhee, S.G.4    Stadtman, E.R.5
  • 30
    • 0030131126 scopus 로고    scopus 로고
    • Expression and cellular localization of rab28 mRNA and Rab28 protein during maize embryogenesis
    • Niogret, M.F., Culiáñez-Macià, F.A., Goday, A., Albà, M.M. and Pagès, M. (1996) Expression and cellular localization of rab28 mRNA and Rab28 protein during maize embryogenesis. Plant J. 9, 549-557.
    • (1996) Plant J. , vol.9 , pp. 549-557
    • Niogret, M.F.1    Culiáñez-Macià, F.A.2    Goday, A.3    Albà, M.M.4    Pagès, M.5
  • 31
    • 0029830579 scopus 로고    scopus 로고
    • Intra-and extra-cellular localization of 'cytosolic' CuZn-superoxide dismutase in spinach leaf and hypocotyl
    • Ogawa, K., Kanematsu, S. and Asada, K. (1996) Intra-and extra-cellular localization of 'cytosolic' CuZn-superoxide dismutase in spinach leaf and hypocotyl. Plant Cell Physiol. 37, 790-799.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 790-799
    • Ogawa, K.1    Kanematsu, S.2    Asada, K.3
  • 32
    • 84974513158 scopus 로고
    • DNA and desiccation tolerance
    • Osborne, D.J. and Boubriak, I.I. (1994) DNA and desiccation tolerance. Seed Sci. Res. 4, 175-185.
    • (1994) Seed Sci. Res. , vol.4 , pp. 175-185
    • Osborne, D.J.1    Boubriak, I.I.2
  • 33
    • 0027297369 scopus 로고
    • Protein localization to the nucleolus: A search for targeting domains in nucleolin
    • Schmidt-Zachmann, M.S. and Nigg, E.A. (1993) Protein localization to the nucleolus: a search for targeting domains in nucleolin. J. Cell Sci. 105, 799-806.
    • (1993) J. Cell Sci. , vol.105 , pp. 799-806
    • Schmidt-Zachmann, M.S.1    Nigg, E.A.2
  • 34
    • 0030237516 scopus 로고    scopus 로고
    • A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains
    • Stacy, R.A.P., Munthe, E., Steinum, T., Sharma, B. and Aalen, R.B. (1996) A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains. Plant Mol. Biol. 31, 1205-1216.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 1205-1216
    • Stacy, R.A.P.1    Munthe, E.2    Steinum, T.3    Sharma, B.4    Aalen, R.B.5
  • 35
    • 0030021536 scopus 로고    scopus 로고
    • Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice
    • Xu, D., Duan, X., Wang, B., Hong, B., Ho, D.T.-H. and Wu, R. (1996) Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice. Plant Physiol. 110, 249-257.
    • (1996) Plant Physiol. , vol.110 , pp. 249-257
    • Xu, D.1    Duan, X.2    Wang, B.3    Hong, B.4    Ho, D.T.-H.5    Wu, R.6


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