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Volumn 218, Issue 3, 2004, Pages 406-416

Characterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters

Author keywords

Anion; Arabidopsis; Chloroplast; Inner envelope; Transporter

Indexed keywords

AMINO ACIDS; CHLOROPHYLL; CYTOLOGY; FLUORESCENCE; GENES; IMMUNOLOGY; PROTEINS;

EID: 0742267789     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-003-1121-5     Document Type: Article
Times cited : (35)

References (50)
  • 1
    • 0031131603 scopus 로고    scopus 로고
    • Characterization of AtSEC12 and AtSAR1. Proteins likely involved in endoplasmic reticulum and golgi transport
    • Bar-Peled M, Raikhel NV (1997) Characterization of AtSEC12 and AtSAR1. proteins likely involved in endoplasmic reticulum and golgi transport. Plant Physiol 114:315-324
    • (1997) Plant Physiol , vol.114 , pp. 315-324
    • Bar-Peled, M.1    Raikhel, N.V.2
  • 2
    • 0032211134 scopus 로고    scopus 로고
    • The localization of the brain-specific inorganic phosphate transporter suggests a specific presynaptic role in glutamatergic transmission
    • Bellocchio EE, Hu H, Pohorille A, Chan J, Pickel VM, Edwards RH (1998) The localization of the brain-specific inorganic phosphate transporter suggests a specific presynaptic role in glutamatergic transmission. J Neurosci 18:8648-8659
    • (1998) J Neurosci , vol.18 , pp. 8648-8659
    • Bellocchio, E.E.1    Hu, H.2    Pohorille, A.3    Chan, J.4    Pickel, V.M.5    Edwards, R.H.6
  • 3
    • 0034637146 scopus 로고    scopus 로고
    • Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter
    • Bellocchio EE, Reimer RJ, Fremeau RT, Edwards RH (2000) Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science 289:957-960
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1    Reimer, R.J.2    Fremeau, R.T.3    Edwards, R.H.4
  • 5
    • 0029896232 scopus 로고    scopus 로고
    • Expression of a renal type I sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions
    • Busch AE, Schuster A, Waldegger S, Wagner CA, Zempel G, Broer S, Biber J, Murer H, Lang F (1996) Expression of a renal type I sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions. Proc Natl Acad Sci USA 93:5347-5351
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5347-5351
    • Busch, A.E.1    Schuster, A.2    Waldegger, S.3    Wagner, C.A.4    Zempel, G.5    Broer, S.6    Biber, J.7    Murer, H.8    Lang, F.9
  • 6
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 6:735-43
    • (1998) Plant J , vol.6 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 7
    • 0028675704 scopus 로고
    • The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homologue of the tonoplast water channel protein TIP
    • Daniels MJ, Mirkov TE, Chrispeels MJ (1994) The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homologue of the tonoplast water channel protein TIP. Plant Physiol 106:1325-1333
    • (1994) Plant Physiol , vol.106 , pp. 1325-1333
    • Daniels, M.J.1    Mirkov, T.E.2    Chrispeels, M.J.3
  • 8
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis SJ, Vierstra RD (1998) Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol Biol 36:521-52
    • (1998) Plant Mol Biol , vol.36 , pp. 521-552
    • Davis, S.J.1    Vierstra, R.D.2
  • 9
    • 0001818570 scopus 로고
    • Purification of the chloroplast
    • Edelman M, Hallick RB, Chua NH (eds). Elsevier, Amsterdam
    • Douce R, Joyard J (1982) Purification of the chloroplast. In: Edelman M, Hallick RB, Chua NH (eds) Methods in chloroplast molecular biology. Elsevier, Amsterdam, pp 239-256
    • (1982) Methods in Chloroplast Molecular Biology , pp. 239-256
    • Douce, R.1    Joyard, J.2
  • 10
    • 85047686510 scopus 로고    scopus 로고
    • The plastidic pentose phosphate translocator represents a link between the cytosolic and the plastidic pentose phosphate pathways in plants
    • Eicks M, Maurino V, Knappe S, Flugge U-I, Fischer K (2002) The plastidic pentose phosphate translocator represents a link between the cytosolic and the plastidic pentose phosphate pathways in plants. Plant Physiol 128:512-522
    • (2002) Plant Physiol , vol.128 , pp. 512-522
    • Eicks, M.1    Maurino, V.2    Knappe, S.3    Flugge, U.-I.4    Fischer, K.5
  • 11
    • 0031397428 scopus 로고    scopus 로고
    • Evidence that a malate/inorganic phosphate exchange translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm
    • Eastmond PJ, Dennis DT, Rawsthorne S (1997) Evidence that a malate/inorganic phosphate exchange translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm. Plant Physiol 114:851-856
    • (1997) Plant Physiol , vol.114 , pp. 851-856
    • Eastmond, P.J.1    Dennis, D.T.2    Rawsthorne, S.3
  • 12
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, von Heijne G (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8:978-984
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 13
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300:1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 16
    • 0036674475 scopus 로고    scopus 로고
    • Transport of carbon in non-green plastids
    • Fischer K, Weber A (2002) Transport of carbon in non-green plastids. Trends Plant Sci 7:345-351
    • (2002) Trends Plant Sci , vol.7 , pp. 345-351
    • Fischer, K.1    Weber, A.2
  • 17
    • 0031105611 scopus 로고    scopus 로고
    • A new class of plastidic phosphate translocators: A putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter
    • Fischer K, Kammerer B, Gutensohn M, Arbinger B, Weber A, Häusler RE, Flügge UI (1997) A new class of plastidic phosphate translocators: a putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter. Plant Cell 9:453-462
    • (1997) Plant Cell , vol.9 , pp. 453-462
    • Fischer, K.1    Kammerer, B.2    Gutensohn, M.3    Arbinger, B.4    Weber, A.5    Häusler, R.E.6    Flügge, U.I.7
  • 18
    • 0024574552 scopus 로고
    • The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: Nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts
    • Flügge UI, Fischer K, Gross A, Sebald W, Lottspeich F, Eckerskorn C (1989) The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts. EMBO J 8:39-46
    • (1989) EMBO J , vol.8 , pp. 39-46
    • Flügge, U.I.1    Fischer, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 19
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman MA, Dush MK, Martin GR (1988) Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85:8998-9002
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 21
    • 0028079979 scopus 로고
    • Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria
    • Heins L, Mentzel H, Schmid A, Benz R, Schmitz UK (1994) Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria. J Biol Chem 269:26402-26410
    • (1994) J Biol Chem , vol.269 , pp. 26402-26410
    • Heins, L.1    Mentzel, H.2    Schmid, A.3    Benz, R.4    Schmitz, U.K.5
  • 22
    • 0742325722 scopus 로고
    • Substrate specificity of the pea chloroplast glycolate transporter
    • Howitz KT, McCarty RE (1985) Substrate specificity of the pea chloroplast glycolate transporter. Biochemistry 24:3645-3650
    • (1985) Biochemistry , vol.24 , pp. 3645-3650
    • Howitz, K.T.1    McCarty, R.E.2
  • 23
    • 0020490258 scopus 로고
    • Characterization of envelope membrane polypeptides from spinach chloroplasts
    • Joyard J, Grossman A, Bartlett SG, Douce R, Chua NH (1982) Characterization of envelope membrane polypeptides from spinach chloroplasts. J Biol Chem 257:1095-1101
    • (1982) J Biol Chem , vol.257 , pp. 1095-1101
    • Joyard, J.1    Grossman, A.2    Bartlett, S.G.3    Douce, R.4    Chua, N.H.5
  • 24
    • 0031834277 scopus 로고    scopus 로고
    • Molecular characterization of a carbon transporter in plastids from heterotrophic tissues: The glucose 6-phosphate/phosphate antiporter
    • Kammerer B, Fischer K, Hilpert B, Schubert S, Gutensohn M, Weber A, Flügge UI (1998) Molecular characterization of a carbon transporter in plastids from heterotrophic tissues: the glucose 6-phosphate/phosphate antiporter. Plant Cell 10:105-117
    • (1998) Plant Cell , vol.10 , pp. 105-117
    • Kammerer, B.1    Fischer, K.2    Hilpert, B.3    Schubert, S.4    Gutensohn, M.5    Weber, A.6    Flügge, U.I.7
  • 25
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport
    • Kim EJ, Zhen RG, Rea PA (1994) Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Proc Natl Acad Sci USA 91:6128-6132
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.G.2    Rea, P.A.3
  • 26
    • 0036800808 scopus 로고    scopus 로고
    • The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles
    • Koo AJK, Ohlrogge JB (2002) The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles. Plant Physiol 130:823-836
    • (2002) Plant Physiol , vol.130 , pp. 823-836
    • Koo, A.J.K.1    Ohlrogge, J.B.2
  • 27
    • 0032959163 scopus 로고    scopus 로고
    • EAT-4, a homolog of a mammalian sodium-dependent inorganic phosphate cotransporter, is necessary for glutamatergic neuro-transmission in Caenorhabditis elegans
    • Lee RY, Sawin ER, Chalfie M, Horvitz HR, Avery L (1999) EAT-4, a homolog of a mammalian sodium-dependent inorganic phosphate cotransporter, is necessary for glutamatergic neuro-transmission in Caenorhabditis elegans. J Neurosci 19:159-167
    • (1999) J Neurosci , vol.19 , pp. 159-167
    • Lee, R.Y.1    Sawin, E.R.2    Chalfie, M.3    Horvitz, H.R.4    Avery, L.5
  • 28
    • 0029775088 scopus 로고    scopus 로고
    • Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane
    • Lübeck J, Soll J, Akita M, Nielsen E, Keegstra K (1996) Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J 15:4230-4238
    • (1996) EMBO J , vol.15 , pp. 4230-4238
    • Lübeck, J.1    Soll, J.2    Akita, M.3    Nielsen, E.4    Keegstra, K.5
  • 29
    • 0018587160 scopus 로고
    • Transport du sulfate à travers la double membrane limitante, ou enveloppe, des chloroplastes d'épinard
    • Mourioux G, Douce R (1979) Transport du sulfate à travers la double membrane limitante, ou enveloppe, des chloroplastes d'épinard. Biochimie 61:1283-1292
    • (1979) Biochimie , vol.61 , pp. 1283-1292
    • Mourioux, G.1    Douce, R.2
  • 30
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Neilsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Neilsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 0030039392 scopus 로고    scopus 로고
    • Unidirectional transport of orthophosphate across the envelope of isolated cauliflower-bud amyloplasts
    • Neuhaus HE, Maass U (1996) Unidirectional transport of orthophosphate across the envelope of isolated cauliflower-bud amyloplasts. Planta 198:542-548
    • (1996) Planta , vol.198 , pp. 542-548
    • Neuhaus, H.E.1    Maass, U.2
  • 32
    • 0034193582 scopus 로고    scopus 로고
    • Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids
    • Neuhaus HE, Wagner R (2000) Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids. Biochim Biophys Acta 1465:307-323
    • (2000) Biochim Biophys Acta , vol.1465 , pp. 307-323
    • Neuhaus, H.E.1    Wagner, R.2
  • 33
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L.
    • Neuhaus HE, Thom E, Möhlmann T, Steup M, Kampfenkel K (1997) Characterization of a novel ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L. Plant J 11:73-82
    • (1997) Plant J , vol.11 , pp. 73-82
    • Neuhaus, H.E.1    Thom, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 36
    • 0030787877 scopus 로고    scopus 로고
    • Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane
    • Pohlmeyer K, Soll J, Steinkamp T, Hinnah S, Wagner R (1997) Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane. Proc Natl Acad Sci USA 94:9504-9509
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9504-9509
    • Pohlmeyer, K.1    Soll, J.2    Steinkamp, T.3    Hinnah, S.4    Wagner, R.5
  • 38
    • 0028149758 scopus 로고
    • Ion channel properties of the reconstituted chloroplast triose phosphate/phosphate translocator
    • Schwarz M, Gross A, Steinkamp T, Flügge UI, Wagner R (1994) Ion channel properties of the reconstituted chloroplast triose phosphate/phosphate translocator. J Biol Chem 269:29481-29489
    • (1994) J Biol Chem , vol.269 , pp. 29481-29489
    • Schwarz, M.1    Gross, A.2    Steinkamp, T.3    Flügge, U.I.4    Wagner, R.5
  • 39
    • 0034648770 scopus 로고    scopus 로고
    • Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons
    • Takamori S, Rhee JS, Rosenmund C, Jahn R (2000) Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons. Nature 407:189-194
    • (2000) Nature , vol.407 , pp. 189-194
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 41
    • 0029053516 scopus 로고
    • A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway
    • Tranel PJ, Froehlich J, Goyal A, Keegstra K (1995) A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. EMBO J 14:2436-2446
    • (1995) EMBO J , vol.14 , pp. 2436-2446
    • Tranel, P.J.1    Froehlich, J.2    Goyal, A.3    Keegstra, K.4
  • 42
    • 0030697430 scopus 로고    scopus 로고
    • A 50-picosiemens anion channel of the chloroplast envelope is involved in chloroplast protein import
    • van den Wijngaard PWJ, Vredenberg WJ (1997) A 50-picosiemens anion channel of the chloroplast envelope is involved in chloroplast protein import. J Biol Chem 272:29430-29433
    • (1997) J Biol Chem , vol.272 , pp. 29430-29433
    • Van Den Wijngaard, P.W.J.1    Vredenberg, W.J.2
  • 44
    • 0036670270 scopus 로고    scopus 로고
    • A chloroplast phosphate transporter, PHT2;1, influences allocation of phosphate within the plant and phosphate-starvation responses
    • Versaw WK, Harrison MJ (2002) A chloroplast phosphate transporter, PHT2;1, influences allocation of phosphate within the plant and phosphate-starvation responses. Plant Cell 14:1751-1766
    • (2002) Plant Cell , vol.14 , pp. 1751-1766
    • Versaw, W.K.1    Harrison, M.J.2
  • 45
    • 0028917799 scopus 로고
    • The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: Molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells
    • Weber A, Menzlaff E, Arbinger B, Gutensohn M, Eckerskorn C, Flügge UI (1995) The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells. Biochemistry 34:2621-2627
    • (1995) Biochemistry , vol.34 , pp. 2621-2627
    • Weber, A.1    Menzlaff, E.2    Arbinger, B.3    Gutensohn, M.4    Eckerskorn, C.5    Flügge, U.I.6
  • 48
    • 0032446940 scopus 로고    scopus 로고
    • +-dependent phosphate cotransporters: The NaPi protein families
    • +-dependent phosphate cotransporters: the NaPi protein families. J Exp Biol 201:3135-3142
    • (1998) J Exp Biol , vol.201 , pp. 3135-3142
    • Werner, A.1    Dehmelt, L.2    Nalbant, P.3
  • 49
    • 0000782157 scopus 로고
    • Glutamine transport and the role of the glutamine translocator in chloroplasts
    • Yu J, Woo KC (1988) Glutamine transport and the role of the glutamine translocator in chloroplasts. Plant Physiol 88:1048-1054
    • (1988) Plant Physiol , vol.88 , pp. 1048-1054
    • Yu, J.1    Woo, K.C.2
  • 50
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N, Kavanaugh MP (1996) Flux coupling in a neuronal glutamate transporter. Nature 383:634-637
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2


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