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Volumn 158, Issue 1, 2007, Pages 46-58

Identification and subcellular localization of the soybean copper P1B-ATPase GmHMA8 transporter

Author keywords

ATPase copper transporter; Cell suspensions; Chloroplast; Immunofluorescence labelling; Immunogold labelling; Soybean; Thylakoid membrane

Indexed keywords

COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; GMHMA8 TRANSPORTER; POLYCLONAL ANTIBODY; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 33947324994     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.10.016     Document Type: Article
Times cited : (44)

References (59)
  • 1
    • 17644403212 scopus 로고    scopus 로고
    • Two P-type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts
    • Abdel-Ghany S.E., Müller-Moulé P., Niyogi K.K., Pilon M., and Shikanai T. Two P-type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts. Plant Cell 17 (2005) 1-19
    • (2005) Plant Cell , vol.17 , pp. 1-19
    • Abdel-Ghany, S.E.1    Müller-Moulé, P.2    Niyogi, K.K.3    Pilon, M.4    Shikanai, T.5
  • 2
    • 33645821051 scopus 로고    scopus 로고
    • Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake
    • Achila D., Banci L., Bertini I., Brunce J., Ciofi-Baffoni S., and Huffman D.L. Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake. Proc. Natl. Acad. Sci. USA 103 (2006) 5729-5734
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5729-5734
    • Achila, D.1    Banci, L.2    Bertini, I.3    Brunce, J.4    Ciofi-Baffoni, S.5    Huffman, D.L.6
  • 3
    • 33644867700 scopus 로고    scopus 로고
    • Projection structure of the human copper transporter CTR1 at 6-Å resolution reveals a compact trimer with a novel channel-like architecture
    • Aller S.G., and Unger V.M. Projection structure of the human copper transporter CTR1 at 6-Å resolution reveals a compact trimer with a novel channel-like architecture. Proc. Natl. Acad. Sci. USA 103 (2006) 3627-3632
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3627-3632
    • Aller, S.G.1    Unger, V.M.2
  • 4
    • 0024988375 scopus 로고
    • Protein database searches for multiple alignments
    • Altschul S.F., and Lipman D.J. Protein database searches for multiple alignments. Proc. Natl. Acad. Sci. USA 87 (1990) 5509-5513
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5509-5513
    • Altschul, S.F.1    Lipman, D.J.2
  • 7
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplast. Polyphenoloxidase in Beta vulgaris
    • Arnon D. Copper enzymes in isolated chloroplast. Polyphenoloxidase in Beta vulgaris. Plant Physiol. 24 (1949) 1-15
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.1
  • 8
    • 0034976968 scopus 로고    scopus 로고
    • Inventory of the superfamily of P-type ion pumps in Arabidopsis
    • Axelsen K.B., and Palmgrem M.G. Inventory of the superfamily of P-type ion pumps in Arabidopsis. Plant Physiol. 126 (2001) 696-706
    • (2001) Plant Physiol. , vol.126 , pp. 696-706
    • Axelsen, K.B.1    Palmgrem, M.G.2
  • 9
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen K.B., and Palmgrem M.G. Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46 (1998) 84-101
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgrem, M.G.2
  • 10
    • 25144462110 scopus 로고    scopus 로고
    • Microspore-derived embryogenesis in Capsicum annuum: subcellular rearrangements through development
    • Barany I., González-Melendi P., Mityko J., Fadón B., Risueño M.C., and Testillano P.S. Microspore-derived embryogenesis in Capsicum annuum: subcellular rearrangements through development. Biol. Cell 97 (2005) 709-722
    • (2005) Biol. Cell , vol.97 , pp. 709-722
    • Barany, I.1    González-Melendi, P.2    Mityko, J.3    Fadón, B.4    Risueño, M.C.5    Testillano, P.S.6
  • 11
    • 33744487632 scopus 로고    scopus 로고
    • Excess copper effect on growth, chloroplast ultrastructure, oxygen-evolution activity and chlorophyll fluorescence in Glycine max cell suspensions
    • Bernal M., Ramiro M.V., Cases R., Picorel R., and Yruela I. Excess copper effect on growth, chloroplast ultrastructure, oxygen-evolution activity and chlorophyll fluorescence in Glycine max cell suspensions. Physiol. Plant 127 (2006) 312-325
    • (2006) Physiol. Plant , vol.127 , pp. 312-325
    • Bernal, M.1    Ramiro, M.V.2    Cases, R.3    Picorel, R.4    Yruela, I.5
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding. Anal. Biochem. 72 (1976) 248-259
    • (1976) Anal. Biochem. , vol.72 , pp. 248-259
    • Bradford, M.M.1
  • 13
    • 0031586003 scopus 로고    scopus 로고
    • Prediction of complete gene structures in human genomic DNA
    • Burge C., and Karlin S. Prediction of complete gene structures in human genomic DNA. J. Mol. Biol. 268 (1997) 78-94
    • (1997) J. Mol. Biol. , vol.268 , pp. 78-94
    • Burge, C.1    Karlin, S.2
  • 14
    • 0035087896 scopus 로고    scopus 로고
    • Molecular mechanisms of plant metal tolerance and homeostasis
    • Clemens S. Molecular mechanisms of plant metal tolerance and homeostasis. Planta 212 (2001) 475-486
    • (2001) Planta , vol.212 , pp. 475-486
    • Clemens, S.1
  • 15
    • 33645754710 scopus 로고    scopus 로고
    • Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations
    • Dmitriev O., Tsivkovskii R., Abildgaard F., Morgan C.T., Markley J.L., and Lutsenko S. Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations. Proc. Natl. Acad. Sci. USA 103 (2006) 5302-5307
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5302-5307
    • Dmitriev, O.1    Tsivkovskii, R.2    Abildgaard, F.3    Morgan, C.T.4    Markley, J.L.5    Lutsenko, S.6
  • 16
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O., Nielsen H., and von Heijne G. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8 (1999) 978-984
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Heijne, G.3
  • 18
    • 0742305196 scopus 로고    scopus 로고
    • Expression of lipoxigenase during organogenic nodule formation from hoop internodes (Humulus lupulus var. Nugget)
    • Fortes A.M., Coronado M.J., Testillano P.S., Risueño M.C., and Pais M.S. Expression of lipoxigenase during organogenic nodule formation from hoop internodes (Humulus lupulus var. Nugget). J. Histochem. Cytochem. 52 (2004) 227-241
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 227-241
    • Fortes, A.M.1    Coronado, M.J.2    Testillano, P.S.3    Risueño, M.C.4    Pais, M.S.5
  • 21
    • 0346752497 scopus 로고    scopus 로고
    • Transition metal transporters in plants
    • Hall J.L., and Williams L.E. Transition metal transporters in plants. J. Exp. Bot. 54 (2003) 2601-2613
    • (2003) J. Exp. Bot. , vol.54 , pp. 2601-2613
    • Hall, J.L.1    Williams, L.E.2
  • 24
    • 0028360414 scopus 로고
    • A copper-transporting P-type ATPase found in thylakoid of the cyanobacterium Synechococcus species PCC7942
    • Kanamaru K., Kashiwagi S., and Mizuno T. A copper-transporting P-type ATPase found in thylakoid of the cyanobacterium Synechococcus species PCC7942. Mol. Microbiol. 13 (1994) 369-377
    • (1994) Mol. Microbiol. , vol.13 , pp. 369-377
    • Kanamaru, K.1    Kashiwagi, S.2    Mizuno, T.3
  • 25
    • 0041837558 scopus 로고    scopus 로고
    • Electron microscopy in cell biology: integrating structure and function
    • Koster A.J., and Klumperman J. Electron microscopy in cell biology: integrating structure and function. Nat. Rev. Mol. Cell Biol. 4 (2003) SS6-SS10
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4
    • Koster, A.J.1    Klumperman, J.2
  • 27
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • Kühlbrandt W. Biology, structure and mechanism of P-type ATPases. Nat. Rev. Mol. Cell Biol. 5 (2004) 282-295
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0027937063 scopus 로고
    • P-type ATPase from the cyanobacterium Synechococcus PCC 7942 related to the human Menkes and Wilson disease gene products
    • Phung L.T., Ajlani G., and KaselKorn R. P-type ATPase from the cyanobacterium Synechococcus PCC 7942 related to the human Menkes and Wilson disease gene products. Proc. Natl. Acad. Sci. USA 91 (1994) 9651-9654
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9651-9654
    • Phung, L.T.1    Ajlani, G.2    KaselKorn, R.3
  • 34
    • 0032845338 scopus 로고    scopus 로고
    • Families of soft-metal-ion-transporting ATPases
    • Rensing M., Ghosh M., and Rosen B.P. Families of soft-metal-ion-transporting ATPases. J. Bacteriol. 181 (1999) 5891-5897
    • (1999) J. Bacteriol. , vol.181 , pp. 5891-5897
    • Rensing, M.1    Ghosh, M.2    Rosen, B.P.3
  • 35
    • 0012785032 scopus 로고    scopus 로고
    • The use of cryomethods for plant biology studies
    • Calderón-Benavides H.A., and Yacamán M.J. (Eds), Inst. Physics, Publ., Bristol, Philadelphia
    • Risueño M.C., Testillano P.S., and González-Melendi P. The use of cryomethods for plant biology studies. In: Calderón-Benavides H.A., and Yacamán M.J. (Eds). Electron Microscopy 98 (1998), Inst. Physics, Publ., Bristol, Philadelphia 3-4
    • (1998) Electron Microscopy 98 , pp. 3-4
    • Risueño, M.C.1    Testillano, P.S.2    González-Melendi, P.3
  • 36
    • 0013689158 scopus 로고
    • Photosynthetic characteristics of a photoautotrophic cell suspension culture of soybean
    • Rogers S.M.D., Ogren W.L., and Widholm J.M. Photosynthetic characteristics of a photoautotrophic cell suspension culture of soybean. Plant Physiol. 84 (1987) 1451-1456
    • (1987) Plant Physiol. , vol.84 , pp. 1451-1456
    • Rogers, S.M.D.1    Ogren, W.L.2    Widholm, J.M.3
  • 42
    • 0002964990 scopus 로고
    • Estimating molecular weights of polypeptides by SDS gel electrophoresis
    • Creighton T.E. (Ed), IRL Press, Oxford University Press
    • See Y.P., and Jackowski G. Estimating molecular weights of polypeptides by SDS gel electrophoresis. In: Creighton T.E. (Ed). Protein Structure a Practical A Approach (1990), IRL Press, Oxford University Press 1-19
    • (1990) Protein Structure a Practical A Approach , pp. 1-19
    • See, Y.P.1    Jackowski, G.2
  • 43
    • 0038102386 scopus 로고    scopus 로고
    • Hsp70 and Hsp90 Change their expression and in situ localization after microspore embryogenesis induction in Brassica napus cv Topas
    • Seguí-Simarro J.M., Testillano P.S., and Risueño M.C. Hsp70 and Hsp90 Change their expression and in situ localization after microspore embryogenesis induction in Brassica napus cv Topas. J. Struct. Biol. 142 (2003) 379-391
    • (2003) J. Struct. Biol. , vol.142 , pp. 379-391
    • Seguí-Simarro, J.M.1    Testillano, P.S.2    Risueño, M.C.3
  • 44
    • 21544478060 scopus 로고    scopus 로고
    • MAP kinases are developmentally regulated during stress-induced microspore embryogenesis in Brassica napus
    • Seguí-Simarro J.M., Testillano P.S., Jouannic S., Henry Y., and Risueño M.C. MAP kinases are developmentally regulated during stress-induced microspore embryogenesis in Brassica napus. Histochem. Cell Biol. 123 (2005) 541-551
    • (2005) Histochem. Cell Biol. , vol.123 , pp. 541-551
    • Seguí-Simarro, J.M.1    Testillano, P.S.2    Jouannic, S.3    Henry, Y.4    Risueño, M.C.5
  • 46
    • 0037781037 scopus 로고    scopus 로고
    • PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts
    • Shikanai T., Müller-Moulé P., Munekage Y., Niyogi K.K., and Pilon M. PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. Plant Cell 15 (2003) 1333-1346
    • (2003) Plant Cell , vol.15 , pp. 1333-1346
    • Shikanai, T.1    Müller-Moulé, P.2    Munekage, Y.3    Niyogi, K.K.4    Pilon, M.5
  • 47
    • 4744370473 scopus 로고    scopus 로고
    • Differential expression and cellular localization of ERKs during organogenic nodule formation from internodes of Humulus lupulus var. Nugget
    • Silva M.S., Fortes A.M., Testillano P.S., Risueño M.C., and Pais S. Differential expression and cellular localization of ERKs during organogenic nodule formation from internodes of Humulus lupulus var. Nugget. Eur. J. Cell Biol. 83 (2004) 425-433
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 425-433
    • Silva, M.S.1    Fortes, A.M.2    Testillano, P.S.3    Risueño, M.C.4    Pais, S.5
  • 48
    • 0030199612 scopus 로고    scopus 로고
    • CPx-ATPases: a class of P-type ATPases that pump heavy metals
    • Solioz M., and Vulpe C. CPx-ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21 (1996) 237-241
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 49
    • 0028847415 scopus 로고
    • The immunolocalization of nuclear antigens during the pollen developmental program and the induction of pollen embryogenesis
    • Testillano P.S., González-Melendi P., Ahmadian P., Fadon B., and Risueño M.C. The immunolocalization of nuclear antigens during the pollen developmental program and the induction of pollen embryogenesis. Exp. Cell Res. 221 (1995) 41-54
    • (1995) Exp. Cell Res. , vol.221 , pp. 41-54
    • Testillano, P.S.1    González-Melendi, P.2    Ahmadian, P.3    Fadon, B.4    Risueño, M.C.5
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0035827547 scopus 로고    scopus 로고
    • Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803
    • Tottey S., Rich P.R., Rondet S.A., and Robinson N.J. Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803. J. Biol. Chem. 276 (2001) 1999-2004
    • (2001) J. Biol. Chem. , vol.276 , pp. 1999-2004
    • Tottey, S.1    Rich, P.R.2    Rondet, S.A.3    Robinson, N.J.4
  • 52
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C., and Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418 (2002) 605-611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 53
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima C., Nakasako M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 54
    • 0028826929 scopus 로고
    • In vitro synthesis and assembly of photosystem II core proteins. The D1 protein can be incorporated into photosystem II in isolated chloroplasts and thylakoids
    • Van Wijk K.J., Bingsmark S., Aro E.M., and Andersson B. In vitro synthesis and assembly of photosystem II core proteins. The D1 protein can be incorporated into photosystem II in isolated chloroplasts and thylakoids. J. Biol. Chem. 270 (1995) 25685-25695
    • (1995) J. Biol. Chem. , vol.270 , pp. 25685-25695
    • Van Wijk, K.J.1    Bingsmark, S.2    Aro, E.M.3    Andersson, B.4
  • 55
    • 6344278744 scopus 로고    scopus 로고
    • Overexpression of AtHMA4 enhances root-to-shoot translocation of zinc and cadmium and plant metal tolerance
    • Verret F., Gravot A., Auroy P., Leonhardt N., Pascale D., Nussaume L., Vavasseur A., and Richaud P. Overexpression of AtHMA4 enhances root-to-shoot translocation of zinc and cadmium and plant metal tolerance. FEBS Lett. 576 (2004) 306-312
    • (2004) FEBS Lett. , vol.576 , pp. 306-312
    • Verret, F.1    Gravot, A.2    Auroy, P.3    Leonhardt, N.4    Pascale, D.5    Nussaume, L.6    Vavasseur, A.7    Richaud, P.8
  • 57
    • 25844489990 scopus 로고    scopus 로고
    • 1B-ATPases-an ancient family of transition metal pumps with diverse functions in plants
    • 1B-ATPases-an ancient family of transition metal pumps with diverse functions in plants. Trends Plant Sci. 10 (2005) 491-502
    • (2005) Trends Plant Sci. , vol.10 , pp. 491-502
    • Williams, LE.1    Mills, R.F.2
  • 58
    • 0034193372 scopus 로고    scopus 로고
    • Emerging mechanisms for heavy metal transport in plants
    • Williams L.E., Pittman J.K., and Hall J.L. Emerging mechanisms for heavy metal transport in plants. Biochim. Biophys. Acta 1465 (2000) 104-126
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 104-126
    • Williams, L.E.1    Pittman, J.K.2    Hall, J.L.3
  • 59
    • 0034025925 scopus 로고    scopus 로고
    • A strong loss of function mutation in RAN1 results in constitutive activation of the ethylene response pathway as well as rosette-lethal phenotype
    • Woeste K.E., and Kieber J.J. A strong loss of function mutation in RAN1 results in constitutive activation of the ethylene response pathway as well as rosette-lethal phenotype. Plant Cell 12 (2000) 443-455
    • (2000) Plant Cell , vol.12 , pp. 443-455
    • Woeste, K.E.1    Kieber, J.J.2


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