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Volumn 16, Issue 8, 2004, Pages 2048-2058

Arabidopsis thaliana GLN2-encoded glutamine synthetase is dual targeted to leaf mitochondria and chloroplasts

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM COMPOUNDS; OXIDATION; PHOTOSYNTHESIS; PROTEINS; PURIFICATION; TISSUE;

EID: 4043103438     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.104.022046     Document Type: Article
Times cited : (143)

References (45)
  • 1
    • 0032504057 scopus 로고    scopus 로고
    • Potential dual targeting of an Arabidopsis archaebacterial-like histidyl-tRNA synthetase to mitochondria and chloroplasts
    • Akashi, K., Grandjean, O., and Small, I. (1998). Potential dual targeting of an Arabidopsis archaebacterial-like histidyl-tRNA synthetase to mitochondria and chloroplasts. FEBS Lett. 431, 39-44.
    • (1998) FEBS Lett. , vol.431 , pp. 39-44
    • Akashi, K.1    Grandjean, O.2    Small, I.3
  • 3
    • 0027435506 scopus 로고
    • In planta Agrobacterium gene transfer by infiltration of adult Arabidopsis thaliana plants
    • Bechtold, N., Ellis, J., and Pelletier, G. (1993). In planta Agrobacterium gene transfer by infiltration of adult Arabidopsis thaliana plants. C. R. Acad. Sci. Paris 316, 1194-1199.
    • (1993) C. R. Acad. Sci. Paris , vol.316 , pp. 1194-1199
    • Bechtold, N.1    Ellis, J.2    Pelletier, G.3
  • 4
    • 0030786960 scopus 로고    scopus 로고
    • Photosynthesis and fluorescence quenching, and the mRNA levels of plastidic glutamine synthetase or of mitochondrial serine hydroxymethyltransferase (SHMT) in the leaves of the wild-type and of the SHMT-deficient stm mutant of Arabidopsis thaliana in relation to the rate of photorespiration
    • Beckmann, K., Dzuibany, C., Biehler, K., Fock, H., Hell, R., Migge, A., and Becken T.W. (1997). Photosynthesis and fluorescence quenching, and the mRNA levels of plastidic glutamine synthetase or of mitochondrial serine hydroxymethyltransferase (SHMT) in the leaves of the wild-type and of the SHMT-deficient stm mutant of Arabidopsis thaliana in relation to the rate of photorespiration. Planta 202, 379-386.
    • (1997) Planta , vol.202 , pp. 379-386
    • Beckmann, K.1    Dzuibany, C.2    Biehler, K.3    Fock, H.4    Hell, R.5    Migge, A.6    Becken, T.W.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0024590390 scopus 로고
    • Channeling of urea cycle intermediates in situ in permeabilized hepatocytes
    • Cheung, C.W., Cohen, N.S., and Raijman, L. (1989). Channeling of urea cycle intermediates in situ in permeabilized hepatocytes. J. Biol. Chem. 264, 4038-4044.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4038-4044
    • Cheung, C.W.1    Cohen, N.S.2    Raijman, L.3
  • 8
    • 0003396888 scopus 로고    scopus 로고
    • The plastidic glutamine synthetase activity is directly modulated by means of redox change at two unique cysteine residues
    • Choi, Y.A., Kim, S.G., and Kwon, V.M. (1999). The plastidic glutamine synthetase activity is directly modulated by means of redox change at two unique cysteine residues. Plant Sci. 149, 175-182.
    • (1999) Plant Sci. , vol.149 , pp. 175-182
    • Choi, Y.A.1    Kim, S.G.2    Kwon, V.M.3
  • 9
    • 0023140949 scopus 로고
    • Channeling of extramitochondrial ornithine to matrix ornithine transcarbamylase
    • Cohen, N.S., Cheung, C.W., and Raijman, L. (1987). Channeling of extramitochondrial ornithine to matrix ornithine transcarbamylase. J. Biol. Chem. 262, 203-208.
    • (1987) J. Biol. Chem. , vol.262 , pp. 203-208
    • Cohen, N.S.1    Cheung, C.W.2    Raijman, L.3
  • 10
    • 0022531131 scopus 로고
    • Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae
    • Davis, R.H. (1986). Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae. Microbiol. Rev. 50, 280-313.
    • (1986) Microbiol. Rev. , vol.50 , pp. 280-313
    • Davis, R.H.1
  • 12
    • 0012795378 scopus 로고
    • Preferential oxidation of glycine by the respiratory chain in pea leaf mitochondria
    • Dry, J.B., Day, D.A., and Wiskich, J.T. (1983). Preferential oxidation of glycine by the respiratory chain in pea leaf mitochondria. FEBS Lett. 158, 154-158.
    • (1983) FEBS Lett. , vol.158 , pp. 154-158
    • Dry, J.B.1    Day, D.A.2    Wiskich, J.T.3
  • 13
    • 0038380988 scopus 로고    scopus 로고
    • Nuclear genes that encode mitochondrial proteins for DNA and RNA metabolism are clustered in the Arabidopsis genome
    • Elo, A., Lyznik, A., Gonzalez, D.O., Kachman, S.D., and Mackenzie, S.A. (2003). Nuclear genes that encode mitochondrial proteins for DNA and RNA metabolism are clustered in the Arabidopsis genome. Plant Cell 15, 1619-1631.
    • (2003) Plant Cell , vol.15 , pp. 1619-1631
    • Elo, A.1    Lyznik, A.2    Gonzalez, D.O.3    Kachman, S.D.4    Mackenzie, S.A.5
  • 14
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and 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
  • 15
    • 0000147690 scopus 로고
    • Urease in jack bean seeds is a cytosolic protein
    • Faye, L., Greenwood, J.S., and Chrispeels, M. (1986). Urease in jack bean seeds is a cytosolic protein. Planta 168, 579-585.
    • (1986) Planta , vol.168 , pp. 579-585
    • Faye, L.1    Greenwood, J.S.2    Chrispeels, M.3
  • 16
    • 0025400542 scopus 로고
    • Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase
    • Freeman, J., Marquez, A., Wallsgrove, R.M., Saarelainen, R., and Forde, B.C. (1990). Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase. Plant Mol. Biol. 14, 297-311.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 297-311
    • Freeman, J.1    Marquez, A.2    Wallsgrove, R.M.3    Saarelainen, R.4    Forde, B.C.5
  • 17
    • 0002047643 scopus 로고
    • Influence of photorespiration on ATP/ADP ratios in the chloroplasts, mitochondria, and cytosol, studied by rapid fractionation of barley (Hordeum vulgare) protoplasts
    • Gardeström, P., and Wigge, B. (1988). Influence of photorespiration on ATP/ADP ratios in the chloroplasts, mitochondria, and cytosol, studied by rapid fractionation of barley (Hordeum vulgare) protoplasts. Plant Physiol. 88, 69-76.
    • (1988) Plant Physiol. , vol.88 , pp. 69-76
    • Gardeström, P.1    Wigge, B.2
  • 18
    • 0032614376 scopus 로고    scopus 로고
    • GFP variants for multispectral imaging of living cells
    • Haseloff, J. (1999). GFP variants for multispectral imaging of living cells. Methods Cell Biol. 58, 139-151.
    • (1999) Methods Cell Biol. , vol.58 , pp. 139-151
    • Haseloff, J.1
  • 19
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • Haseloff, J., Siemering, K.R., Prasher, D.C., and Hodge, S. (1997). Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl. Acad. Sci. USA 94, 2122-2127.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 20
    • 0023013578 scopus 로고
    • Sulfonylurea-resistant mutants of Arabidopsis thaliana
    • Haughn, G., and Somerville, C. (1986). Sulfonylurea-resistant mutants of Arabidopsis thaliana. Mol. Gen. Genet. 204, 430-438.
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 430-438
    • Haughn, G.1    Somerville, C.2
  • 21
    • 0000401603 scopus 로고
    • The chloroplast envelope: Structure, function and role in leaf metabolism
    • Heber, U., and Heldt, H.W. (1981). The chloroplast envelope: Structure, function and role in leaf metabolism. Annu. Rev. Plant Physiol. 32, 139-168.
    • (1981) Annu. Rev. Plant Physiol. , vol.32 , pp. 139-168
    • Heber, U.1    Heldt, H.W.2
  • 22
    • 0034330546 scopus 로고    scopus 로고
    • One RNA polymerase serving two genomes
    • Hedtke, B., Börner, T., and Weihe, A. (2000). One RNA polymerase serving two genomes. EMBO Rep. 1, 435-440.
    • (2000) EMBO Rep. , vol.1 , pp. 435-440
    • Hedtke, B.1    Börner, T.2    Weihe, A.3
  • 23
    • 0032004983 scopus 로고    scopus 로고
    • The protein translocation apparatus of chloroplast envelopes
    • Heins, L., Collinson, I., and Soll, J. (1998). The protein translocation apparatus of chloroplast envelopes. Trends Plant Sci. 3, 56-61.
    • (1998) Trends Plant Sci. , vol.3 , pp. 56-61
    • Heins, L.1    Collinson, I.2    Soll, J.3
  • 24
    • 0030332781 scopus 로고    scopus 로고
    • A probabilistic classification system for predicting the cellular localization sites of proteins
    • Horton, P., and Nakai, K. (1996). A probabilistic classification system for predicting the cellular localization sites of proteins. Int. Syst. Mol. Biol. 4, 109-115.
    • (1996) Int. Syst. Mol. Biol. , vol.4 , pp. 109-115
    • Horton, P.1    Nakai, K.2
  • 25
    • 0029822746 scopus 로고    scopus 로고
    • Targeting presequence acquisition after mitochondrial gene transfer to the nucleus occurs by duplication of existing targeting signals
    • Kadowaki, K., Kubo, N., Ozawa, K., and Hirai, A. (1996). Targeting presequence acquisition after mitochondrial gene transfer to the nucleus occurs by duplication of existing targeting signals. EMBO J. 15, 6652-6661.
    • (1996) EMBO J. , vol.15 , pp. 6652-6661
    • Kadowaki, K.1    Kubo, N.2    Ozawa, K.3    Hirai, A.4
  • 26
    • 0003065251 scopus 로고
    • A critical consideration of the quantum yield of Chlorella-photosynthesis
    • Kok, B. (1948). A critical consideration of the quantum yield of Chlorella-photosynthesis. Enzymologia 13, 1-36.
    • (1948) Enzymologia , vol.13 , pp. 1-36
    • Kok, B.1
  • 27
    • 12044259115 scopus 로고
    • Mitochondrial contribution to photosynthetic metabolism
    • Krömer, S., Malmberg, G., and Gardeström, P. (1993). Mitochondrial contribution to photosynthetic metabolism. Plant Physiol. 102, 947-955.
    • (1993) Plant Physiol. , vol.102 , pp. 947-955
    • Krömer, S.1    Malmberg, G.2    Gardeström, P.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0026344773 scopus 로고
    • A transformation competent genome library in Arabidopsis
    • Lazo, G.R., Stein, P.A., and Ludwig, R.A. (1991). A transformation competent genome library in Arabidopsis. Biotechnology 9, 963-971.
    • (1991) Biotechnology , vol.9 , pp. 963-971
    • Lazo, G.R.1    Stein, P.A.2    Ludwig, R.A.3
  • 30
    • 0002089333 scopus 로고
    • The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.: Nucleotide sequence, expression in different organs and uptake into isolated chloroplasts
    • Lightfoot, D.A., Green, N.K., and Cullimore, J.V. (1988). The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.: Nucleotide sequence, expression in different organs and uptake into isolated chloroplasts. Plant Mol. Biol. 11, 191-202.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 191-202
    • Lightfoot, D.A.1    Green, N.K.2    Cullimore, J.V.3
  • 31
    • 0027539328 scopus 로고
    • Arabidopsis chloroplasts dissimilate L-arginine and L-citrulline for use as N source
    • Ludwig, R.A. (1993). Arabidopsis chloroplasts dissimilate L-arginine and L-citrulline for use as N source. Plant Physiol. 101, 429-435.
    • (1993) Plant Physiol. , vol.101 , pp. 429-435
    • Ludwig, R.A.1
  • 32
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thio-redoxin
    • Motohashi, K., Kondoh, A., Stumpp, M.T., and Hisabori, T. (2001). Comprehensive survey of proteins targeted by chloroplast thio-redoxin. Proc. Natl. Acad. Sci. USA 98, 11224-11229.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 33
    • 0033909566 scopus 로고    scopus 로고
    • Protein sorting signals and prediction of subcellular localization
    • Nakai, K. (2000). Protein sorting signals and prediction of subcellular localization. Adv. Protein Chem. 54, 277-344.
    • (2000) Adv. Protein Chem. , vol.54 , pp. 277-344
    • Nakai, K.1
  • 34
    • 0022397939 scopus 로고
    • Carbamoyl-phosphate synthetases from Neurospora crassa. Immunological relatedness of the enzymes from Neurospora, bacteria, yeast, and mammals
    • Ness, S.A., and Weiss, R.L. (1985). Carbamoyl-phosphate synthetases from Neurospora crassa. Immunological relatedness of the enzymes from Neurospora, bacteria, yeast, and mammals. J. Biol. Chem. 260, 14355-14362.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14355-14362
    • Ness, S.A.1    Weiss, R.L.2
  • 35
    • 0000443883 scopus 로고
    • Photorespiration pathways: Regulation and modification
    • Ogren, W.L. (1984). Photorespiration pathways: Regulation and modification. Annu. Rev. Plant Physiol. 35, 415-442.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 415-442
    • Ogren, W.L.1
  • 36
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • Peeters, N., and Small, I. (2001). Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 1541, 54-63.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 37
    • 0026005555 scopus 로고
    • The glutamine synthetase gene family of Arabidopsis thaliana: Light-regulation and differential expression in leaves, roots and seeds
    • Peterman, T.K., and Goodman, H.M. (1991). The glutamine synthetase gene family of Arabidopsis thaliana: Light-regulation and differential expression in leaves, roots and seeds. Mol. Gen. Genet. 230, 145-154.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 145-154
    • Peterman, T.K.1    Goodman, H.M.2
  • 38
    • 0001151587 scopus 로고    scopus 로고
    • Participation of mitochondrial metabolism in photorespiration. Reconstituted system of peroxisomes and mitochondria from spinach leaves
    • Raghavendra, A.S., Reumann, S., and Heldt, H.W. (1998). Participation of mitochondrial metabolism in photorespiration. Reconstituted system of peroxisomes and mitochondria from spinach leaves. Plant Physiol. 116, 1333-1337.
    • (1998) Plant Physiol. , vol.116 , pp. 1333-1337
    • Raghavendra, A.S.1    Reumann, S.2    Heldt, H.W.3
  • 39
    • 77956999268 scopus 로고
    • Glutamine synthetase (E. coli)
    • Shapiro, B.M., and Stadtman, E.R. (1970). Glutamine synthetase (E. coli). Meth. Enzymol. 17A, 910-922.
    • (1970) Meth. Enzymol. , vol.17 A , pp. 910-922
    • Shapiro, B.M.1    Stadtman, E.R.2
  • 40
    • 0000784788 scopus 로고
    • Inhibition of photosynthesis in Arabidopsis thaliana mutants lacking leaf glutamate synthase
    • Somerville, C.R., and Ogren, W.L. (1980). Inhibition of photosynthesis in Arabidopsis thaliana mutants lacking leaf glutamate synthase. Nature 286, 257-259.
    • (1980) Nature , vol.286 , pp. 257-259
    • Somerville, C.R.1    Ogren, W.L.2
  • 41
    • 0014668307 scopus 로고
    • A chloroplast cytoplasmic shuttle and the reduction of extraplastid NAD
    • Stocking, C.R., and Larson, S. (1969). A chloroplast cytoplasmic shuttle and the reduction of extraplastid NAD. Biochem. Biophys. Res. Commun. 37, 278-282.
    • (1969) Biochem. Biophys. Res. Commun. , vol.37 , pp. 278-282
    • Stocking, C.R.1    Larson, S.2
  • 42
    • 0024288152 scopus 로고
    • Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo
    • Tingey, S., Tsai, F., Edwards, J., Walker, E., and Coruzzi, G. (1983). Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo. J. Biol. Chem. 263, 9651-9657.
    • (1983) J. Biol. Chem. , vol.263 , pp. 9651-9657
    • Tingey, S.1    Tsai, F.2    Edwards, J.3    Walker, E.4    Coruzzi, G.5
  • 43
    • 0028984192 scopus 로고
    • Cis elements and trans-acting factors affecting regulation of a nonphotosynthetic light-regulated gene for chloroplast glutamine synthetase
    • Tjaden, G., Edwards, J.W., and Coruzzi, G.M. (1995). Cis elements and trans-acting factors affecting regulation of a nonphotosynthetic light-regulated gene for chloroplast glutamine synthetase. Plant Physiol. 108, 1109-1117.
    • (1995) Plant Physiol. , vol.108 , pp. 1109-1117
    • Tjaden, G.1    Edwards, J.W.2    Coruzzi, G.M.3
  • 44
    • 0034671866 scopus 로고    scopus 로고
    • The origins of genomic duplications in Arabidopsis
    • Vision, T.J., Brown, D.G., and Tanksley, S.D. (2000). The origins of genomic duplications in Arabidopsis. Science 290, 2114-2117.
    • (2000) Science , vol.290 , pp. 2114-2117
    • Vision, T.J.1    Brown, D.G.2    Tanksley, S.D.3
  • 45
    • 0004502820 scopus 로고
    • Glycine decarboxylation in mitochondria isolated from spinach leaves
    • Woo, K.C., and Osmond, C.B. (1976). Glycine decarboxylation in mitochondria isolated from spinach leaves. Aust. J. Plant Physiol. 3, 771-785.
    • (1976) Aust. J. Plant Physiol. , vol.3 , pp. 771-785
    • Woo, K.C.1    Osmond, C.B.2


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