메뉴 건너뛰기




Volumn 8, Issue 1, 2008, Pages 149-159

Early manganese-toxicity response in Vigna unguiculata L. - A proteomic and transcriptomic study

Author keywords

Apoplast; Cowpea; Manganese toxicity; Symplast

Indexed keywords

MANGANESE;

EID: 38149040209     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700478     Document Type: Article
Times cited : (74)

References (54)
  • 1
    • 0000559963 scopus 로고
    • Webb, M. J, Nable, R. O, Graham, R. D, Hannam, R. J, Eds, Kluwer Academic Publishers, Dodrecht/Boston/London
    • Burnell, J. N., in: Webb, M. J., Nable, R. O., Graham, R. D., Hannam, R. J. (Eds.), Manganese in Soil and Plants, Kluwer Academic Publishers, Dodrecht/Boston/London 1988, pp. 125-137.
    • (1988) Manganese in Soil and Plants , pp. 125-137
    • Burnell, J.N.1
  • 3
    • 0000255924 scopus 로고
    • Webb, M. J, Nable, R. O, Graham, R. D, Hannam, R. J, Eds, Kluwer Academic Publishers, Dodrecht/Boston/London
    • Horst, W. J., in: Webb, M. J., Nable, R. O., Graham, R. D., Hannam, R. J. (Eds.), Manganese in Soil and Plants, Kluwer Academic Publishers, Dodrecht/Boston/London 1988, pp. 175-188.
    • (1988) Manganese in Soil and Plants , pp. 175-188
    • Horst, W.J.1
  • 5
    • 0031968287 scopus 로고    scopus 로고
    • Manganese toxicity in plants
    • El-Jaoual, T., Cox, D. A., Manganese toxicity in plants. J. Plant Nutr. 1998, 21, 353-386.
    • (1998) J. Plant Nutr , vol.21 , pp. 353-386
    • El-Jaoual, T.1    Cox, D.A.2
  • 6
    • 0038571254 scopus 로고
    • Genotypische Unterschiede in der Mangan-Toleranz von Cowpea (Vigna unguiculata)
    • Horst, W. J., Genotypische Unterschiede in der Mangan-Toleranz von Cowpea (Vigna unguiculata). Angew. Bot. 1980, 54, 377-392.
    • (1980) Angew. Bot , vol.54 , pp. 377-392
    • Horst, W.J.1
  • 7
    • 0020870556 scopus 로고
    • Factors responsible for genotypic manganese tolerance in cowpea (Vigna unguiculata)
    • Horst, W. J., Factors responsible for genotypic manganese tolerance in cowpea (Vigna unguiculata). Plant Soil 1983, 72, 213-218.
    • (1983) Plant Soil , vol.72 , pp. 213-218
    • Horst, W.J.1
  • 8
    • 84979375040 scopus 로고
    • Symptome von Manganüberschuss bei Bohnen (Phaseolus vulgaris L.)
    • Horst, W. J., Marschner, H., Symptome von Manganüberschuss bei Bohnen (Phaseolus vulgaris L.). Z. Pflanzenernähr. Bodenk. 1987, 141, 129-142.
    • (1987) Z. Pflanzenernähr. Bodenk , vol.141 , pp. 129-142
    • Horst, W.J.1    Marschner, H.2
  • 9
    • 0004961565 scopus 로고
    • Quick screening of cowpea genotypes for manganese tolerance during vegetative and reproductive growth
    • Horst, W. J., Quick screening of cowpea genotypes for manganese tolerance during vegetative and reproductive growth. Z. Pflanzenernähr. Bodenk. 1982, 145, 423-435.
    • (1982) Z. Pflanzenernähr. Bodenk , vol.145 , pp. 423-435
    • Horst, W.J.1
  • 10
    • 0001135795 scopus 로고
    • Effect of light intensity on manganese toxicity symptoms and callose formation in cowpea (Vigna unguiculata (L.) Walp.)
    • Wissemeier, A. H., Horst, W. J., Effect of light intensity on manganese toxicity symptoms and callose formation in cowpea (Vigna unguiculata (L.) Walp.). Plant Soil 1992, 143, 299-309.
    • (1992) Plant Soil , vol.143 , pp. 299-309
    • Wissemeier, A.H.1    Horst, W.J.2
  • 11
    • 0038625040 scopus 로고    scopus 로고
    • Apoplastic peroxidase and ascorbate are involved in manganese toxicity and tolerance of Vigna unguiculata
    • Fecht-Christoffers, M. M., Maier, P., Horst, W. J., Apoplastic peroxidase and ascorbate are involved in manganese toxicity and tolerance of Vigna unguiculata. Physiol. Plant. 2003a, 117, 237-244.
    • (2003) Physiol. Plant , vol.117 , pp. 237-244
    • Fecht-Christoffers, M.M.1    Maier, P.2    Horst, W.J.3
  • 12
    • 33745471473 scopus 로고    scopus 로고
    • The role of hydrogen peroxide-producing and hydrogen peroxide-consuming peroxidases in the leaf apoplast of cowpea in manganese tolerance
    • Fecht-Christoffers, M. M., Führs, H., Braun, H.-P., Horst, W. J., The role of hydrogen peroxide-producing and hydrogen peroxide-consuming peroxidases in the leaf apoplast of cowpea in manganese tolerance. Plant Physiol. 2006, 140, 1451-1463.
    • (2006) Plant Physiol , vol.140 , pp. 1451-1463
    • Fecht-Christoffers, M.M.1    Führs, H.2    Braun, H.-P.3    Horst, W.J.4
  • 15
    • 34347219445 scopus 로고    scopus 로고
    • A scretory pathway-localized cation diffusion facilitator confers plant manganese tolerance
    • Peiter, E., Montanini, B., Gobert, A., Pedas, P. et al., A scretory pathway-localized cation diffusion facilitator confers plant manganese tolerance. Proc. Natl. Acad. Sci. USA 2007, 104, 8532-8537.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8532-8537
    • Peiter, E.1    Montanini, B.2    Gobert, A.3    Pedas, P.4
  • 16
    • 0038028683 scopus 로고    scopus 로고
    • Genes encoding proteins of the Cation Diffusion Facilitator family that confer manganese tolerance
    • Delhaize, E., Kataoka, T., Hebb, D. M., White, R. G., Ryan, R., Genes encoding proteins of the Cation Diffusion Facilitator family that confer manganese tolerance. Plant Cell 2003, 15, 1131-1142.
    • (2003) Plant Cell , vol.15 , pp. 1131-1142
    • Delhaize, E.1    Kataoka, T.2    Hebb, D.M.3    White, R.G.4    Ryan, R.5
  • 17
    • 0033833640 scopus 로고    scopus 로고
    • Expression of Arabidopsis CAX2 in tobacco. Altered metal accumulation and increased manganese tolerance
    • Hirschi, K. D., Korenkov, V. D., Wilganowski, N. L., Wagner, G. J., Expression of Arabidopsis CAX2 in tobacco. Altered metal accumulation and increased manganese tolerance. Plant Physiol. 2000, 124, 125-133.
    • (2000) Plant Physiol , vol.124 , pp. 125-133
    • Hirschi, K.D.1    Korenkov, V.D.2    Wilganowski, N.L.3    Wagner, G.J.4
  • 18
  • 20
    • 1642586812 scopus 로고    scopus 로고
    • Subcellular and tissue Mn compartmentation in bean leaves under Mn toxicity stress
    • González, A., Lynch, J. P., Subcellular and tissue Mn compartmentation in bean leaves under Mn toxicity stress. Aust. J. Plant Physiol. 1999, 26, 811-822.
    • (1999) Aust. J. Plant Physiol , vol.26 , pp. 811-822
    • González, A.1    Lynch, J.P.2
  • 21
    • 9644291398 scopus 로고    scopus 로고
    • Manganese accumulation in rice: Implications for photosynthetic functioning
    • Lidon, F. C., Barreiro, M. G., Ramalho, J. C., Manganese accumulation in rice: implications for photosynthetic functioning. J. Plant Physiol. 2004, 161, 1235-1244.
    • (2004) J. Plant Physiol , vol.161 , pp. 1235-1244
    • Lidon, F.C.1    Barreiro, M.G.2    Ramalho, J.C.3
  • 22
    • 0031415729 scopus 로고    scopus 로고
    • 2 assimilation of contrating common bean genotypes
    • 2 assimilation of contrating common bean genotypes. Physiol. Plant. 1997, 101, 872-880.
    • (1997) Physiol. Plant , vol.101 , pp. 872-880
    • González, A.1    Lynch, J.P.2
  • 23
    • 0000181468 scopus 로고    scopus 로고
    • Light and excess manganese: Implications for oxidative stress in common bean
    • González, A., Steffen, K. L., Lynch, J. P., Light and excess manganese: Implications for oxidative stress in common bean. Plant Physiol. 1998, 118, 493-504.
    • (1998) Plant Physiol , vol.118 , pp. 493-504
    • González, A.1    Steffen, K.L.2    Lynch, J.P.3
  • 24
    • 0001173652 scopus 로고
    • Evidence for effects on the in vivo activity of ribulose-bisphosphate carboxylase/ oxygenase during development of Mn toxicity in tobacco
    • Houtz, R. L., Nable, R. O., Cheniae, G. M., Evidence for effects on the in vivo activity of ribulose-bisphosphate carboxylase/ oxygenase during development of Mn toxicity in tobacco. Plant Physiol. 1988, 86, 1143-1149.
    • (1988) Plant Physiol , vol.86 , pp. 1143-1149
    • Houtz, R.L.1    Nable, R.O.2    Cheniae, G.M.3
  • 25
    • 0001173651 scopus 로고
    • Early inhibition of photosynthesis during development of Mn toxicity in tobacco
    • Nable, R. O., Houtz, R. L., Cheniae, G. M., Early inhibition of photosynthesis during development of Mn toxicity in tobacco. Plant Physiol. 1988, 86, 1136-1142.
    • (1988) Plant Physiol , vol.86 , pp. 1136-1142
    • Nable, R.O.1    Houtz, R.L.2    Cheniae, G.M.3
  • 26
    • 51249170874 scopus 로고
    • Chlorophyll content and leaf elongation rate in wheat seedlings as a measure of manganese tolerance
    • Moroni, J. S., Briggs, K. G., Taylor, G. J., Chlorophyll content and leaf elongation rate in wheat seedlings as a measure of manganese tolerance. Plant Soil 1991, 136, 1-9.
    • (1991) Plant Soil , vol.136 , pp. 1-9
    • Moroni, J.S.1    Briggs, K.G.2    Taylor, G.J.3
  • 27
    • 33645062273 scopus 로고    scopus 로고
    • Conn, M, Ed, Humana Press, Totowa
    • Mihr, C., Braun, H.-P., in: Conn, M. (Ed.), Handbook of Proteomics, Humana Press, Totowa 2003, pp. 409-416.
    • (2003) Handbook of Proteomics , pp. 409-416
    • Mihr, C.1    Braun, H.-P.2
  • 28
    • 3242754429 scopus 로고    scopus 로고
    • Proteomic approach to characterize the supra-molecular organization of photosystems in higher plants
    • Heinemeyer, J., Eubel, H., Wehmhöner, D., Jänsch, L., Braun, H.-P., Proteomic approach to characterize the supra-molecular organization of photosystems in higher plants. Phytochemistry 2004, 65, 1683-1692.
    • (2004) Phytochemistry , vol.65 , pp. 1683-1692
    • Heinemeyer, J.1    Eubel, H.2    Wehmhöner, D.3    Jänsch, L.4    Braun, H.-P.5
  • 29
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the michondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis
    • Werhahn, W., Braun, H.-P., Biochemical dissection of the michondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 2002, 23, 640-646.
    • (2002) Electrophoresis , vol.23 , pp. 640-646
    • Werhahn, W.1    Braun, H.-P.2
  • 30
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166, 368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 32
    • 37549042703 scopus 로고    scopus 로고
    • Thiellement, H, Zivy, M, Damerval, C, Méchin, V, Eds, Humana Press Inc, Totowa, NJ
    • Heinemeyer, J., Lewejohann, D., Braun, H.-P., in: Thiellement, H., Zivy, M., Damerval, C., Méchin, V. (Eds.), Plant Proteomics: Methods and Protocols, Humana Press Inc., Totowa, NJ 2007, pp. 343-352.
    • (2007) Plant Proteomics: Methods and Protocols , pp. 343-352
    • Heinemeyer, J.1    Lewejohann, D.2    Braun, H.-P.3
  • 33
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: A systematic analysis
    • Neuhoff, V., Stamm, R., Eibl, H., Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: A systematic analysis. Electrophoresis 1985, 6, 427-448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 34
    • 0025320429 scopus 로고
    • Essential problems in quantification of proteins following colloidal staining with Coomassie Brilliant Blue dyes in polyacrylamide gels, and their solution
    • Neuhoff, V., Stamm, R., Pardowitz, I., Arold, N. et al., Essential problems in quantification of proteins following colloidal staining with Coomassie Brilliant Blue dyes in polyacrylamide gels, and their solution. Electrophoresis 1990, 11, 101-117.
    • (1990) Electrophoresis , vol.11 , pp. 101-117
    • Neuhoff, V.1    Stamm, R.2    Pardowitz, I.3    Arold, N.4
  • 35
    • 27144505199 scopus 로고    scopus 로고
    • Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress
    • Castro, A. J., Carapito, C., Zorn, N., Magne, C. et al., Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress. J. Exp. Bot. 2005, 56, 2783-2795.
    • (2005) J. Exp. Bot , vol.56 , pp. 2783-2795
    • Castro, A.J.1    Carapito, C.2    Zorn, N.3    Magne, C.4
  • 36
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko, A., Sunyaev, S., Loboda, A., Shevchenko, A. et al., Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem. 2001, 73, 1917-1926.
    • (2001) Anal. Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4
  • 37
    • 15844428981 scopus 로고    scopus 로고
    • Suppression subtractive hybridization: A method for generating differentially regulated or tissue-specific cDNA probes and libraries
    • Diatchenko, L., Lau, Y. F., Campbell, A. P., Chenchik, A. et al., Suppression subtractive hybridization: a method for generating differentially regulated or tissue-specific cDNA probes and libraries. Proc. Natl. Acad. Sci. USA 1996, 93, 6025-6030.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6025-6030
    • Diatchenko, L.1    Lau, Y.F.2    Campbell, A.P.3    Chenchik, A.4
  • 38
    • 12244283700 scopus 로고    scopus 로고
    • Wulf, A., Manthey, K., Doll, J., Perlick, A. M. et al., Transcriptional changes in response to arbuscular mycorrhiza development in the model plant Medicago truncatula. Mol. Plant Microbe Interact. 2003, 16, 306-314.
    • Wulf, A., Manthey, K., Doll, J., Perlick, A. M. et al., Transcriptional changes in response to arbuscular mycorrhiza development in the model plant Medicago truncatula. Mol. Plant Microbe Interact. 2003, 16, 306-314.
  • 39
    • 0035653682 scopus 로고    scopus 로고
    • Haldrup, A., Jensen, P. E., Lunde, C., Scheller, H. V., Balance of power: A view of the mechanism of photosynthetic state transitions. Trends Plant Sci. 2001, 6, 301-305.
    • Haldrup, A., Jensen, P. E., Lunde, C., Scheller, H. V., Balance of power: A view of the mechanism of photosynthetic state transitions. Trends Plant Sci. 2001, 6, 301-305.
  • 41
    • 0033644689 scopus 로고    scopus 로고
    • Current perspectives on the structure/function basis for regulation and catalysis
    • Miziorko, H. M., Phosphoribulokinase: Current perspectives on the structure/function basis for regulation and catalysis. Adv. Enzymol. Relat. Areas Mol. Biol. 2000, 74, 95-127.
    • (2000) Adv. Enzymol. Relat. Areas Mol. Biol , vol.74 , pp. 95-127
    • Miziorko, H.1    Phosphoribulokinase, M.2
  • 42
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R. S., Viitanen, P. V., Vierling, E., Molecular chaperones and protein folding in plants. Plant Mol. Biol. 1996, 32, 191-222.
    • (1996) Plant Mol. Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 43
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase - Rubisco's catalytic chaperone
    • Portis, A. R., Jr., Rubisco activase - Rubisco's catalytic chaperone. Photosynth. Res. 2003, 75, 11-27.
    • (2003) Photosynth. Res , vol.75 , pp. 11-27
    • Portis Jr., A.R.1
  • 44
    • 1942440433 scopus 로고    scopus 로고
    • The evolutionary development of the protein complement of photosystem 2
    • Raymond, J., Blankenship, R. E., The evolutionary development of the protein complement of photosystem 2. Biochim. Biophys. Acta 2004, 1655, 133-139.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 133-139
    • Raymond, J.1    Blankenship, R.E.2
  • 45
    • 30344437393 scopus 로고    scopus 로고
    • PsbP protein, but not PsbQ protein, is essential for the regulation and stabilization of photosystem II in higher plants
    • Ifuku, K., Yamamoto, Y., Ono, T. A., Ishihara, S., Sato, F., PsbP protein, but not PsbQ protein, is essential for the regulation and stabilization of photosystem II in higher plants. Plant Physiol. 2005, 139, 1175-1184.
    • (2005) Plant Physiol , vol.139 , pp. 1175-1184
    • Ifuku, K.1    Yamamoto, Y.2    Ono, T.A.3    Ishihara, S.4    Sato, F.5
  • 46
    • 18144430898 scopus 로고    scopus 로고
    • The manganese-stabilizing protein is required for photosystem II assembly/stability and photoautotrophy in higher plants
    • Yi, X., McChargue, M., Laborde, S., Frankel, L. K., Bricker, T. M., The manganese-stabilizing protein is required for photosystem II assembly/stability and photoautotrophy in higher plants. J. Biol. Chem. 2005, 280, 16170-16174.
    • (2005) J. Biol. Chem , vol.280 , pp. 16170-16174
    • Yi, X.1    McChargue, M.2    Laborde, S.3    Frankel, L.K.4    Bricker, T.M.5
  • 47
    • 4043148624 scopus 로고    scopus 로고
    • Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem ii activity in the cyanobacterium Synechocystis 6803
    • Thornton, L. E., Ohkawa, H., Roose, J. L., Kashino, Y. et al., Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem ii activity in the cyanobacterium Synechocystis 6803. Plant Cell 2004, 16, 2164-2175.
    • (2004) Plant Cell , vol.16 , pp. 2164-2175
    • Thornton, L.E.1    Ohkawa, H.2    Roose, J.L.3    Kashino, Y.4
  • 48
    • 12144270027 scopus 로고    scopus 로고
    • PsbQ (SII1638) in Synechocystis sp. PCC 6803 is required for photosystem II activity in specific mutants and in nutrient-limiting conditions
    • Summerfield, T. C., Shand, J. A., Bentley, F. K., Eaton-Rye, J. J., PsbQ (SII1638) in Synechocystis sp. PCC 6803 is required for photosystem II activity in specific mutants and in nutrient-limiting conditions. Biochemistry 2005, 44, 805-815.
    • (2005) Biochemistry , vol.44 , pp. 805-815
    • Summerfield, T.C.1    Shand, J.A.2    Bentley, F.K.3    Eaton-Rye, J.J.4
  • 50
    • 2242482888 scopus 로고    scopus 로고
    • A light-dependent mechanism for massive accumulation of manganese in the photosynthetic bacterium Synechocystis sp. PCC 6803
    • Keren, N., Kidd, M. J., Penner-Hahn, J. E., Pakrasi, H. B., A light-dependent mechanism for massive accumulation of manganese in the photosynthetic bacterium Synechocystis sp. PCC 6803. Biochemistry 2002, 41, 15085-15092.
    • (2002) Biochemistry , vol.41 , pp. 15085-15092
    • Keren, N.1    Kidd, M.J.2    Penner-Hahn, J.E.3    Pakrasi, H.B.4
  • 51
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • van Loon, L. C., van Strien, E. A., The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol. 1999, 55, 85-97.
    • (1999) Physiol. Mol. Plant Pathol , vol.55 , pp. 85-97
    • van Loon, L.C.1    van Strien, E.A.2
  • 52
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • van Loon, L. C., Rep, M., Pieterse, C. M., Significance of inducible defense-related proteins in infected plants. Annu. Rev. Phytopathol. 2006, 44, 135-162.
    • (2006) Annu. Rev. Phytopathol , vol.44 , pp. 135-162
    • van Loon, L.C.1    Rep, M.2    Pieterse, C.M.3
  • 53
    • 17444420139 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and plant development
    • Moon, J., Parry, G., Estelle, M., The ubiquitin-proteasome pathway and plant development. Plant Cell 2004, 16, 3181-3195.
    • (2004) Plant Cell , vol.16 , pp. 3181-3195
    • Moon, J.1    Parry, G.2    Estelle, M.3
  • 54
    • 0034851645 scopus 로고    scopus 로고
    • Cryptogein affects expression of α3, α6 and β1 20S proteasome subunits encoding genes in tobacco
    • Dahan, J., Etienne, P., Petitot, A.-S., Houot, V. et al., Cryptogein affects expression of α3, α6 and β1 20S proteasome subunits encoding genes in tobacco. J. Exp. Bot. 2001, 52, 1947-1948.
    • (2001) J. Exp. Bot , vol.52 , pp. 1947-1948
    • Dahan, J.1    Etienne, P.2    Petitot, A.-S.3    Houot, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.