메뉴 건너뛰기




Volumn 45, Issue 1, 2006, Pages 71-82

Antisense reduction of serine hydroxymethyltransferase results in diurnal displacement of NH4+ assimilation in leaves of Solanum tuberosum

Author keywords

Glutamate synthase; Glutamine synthetase; Nitrogen; Photorespiration; Solanum tuberosum; Subunit composition

Indexed keywords

CATALYSIS; PLANTS (BOTANY);

EID: 33644872172     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2005.02598.x     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0030786960 scopus 로고    scopus 로고
    • Photosynthesis and fluorescence quenching, and the mRNA level of plastidic glutamine synthetase or of mitochondrial serine hydroxymethyltransferase (SHMT) in the leaves of the wild type and of the SHMT-deficient mutant of Arabidopsis thaliana in relation to the rate of photorespiration
    • Beckmann K. Dzuibany C. Biehler K. Fock H. Hell R. Migge A. Becker T.W. 1997 Photosynthesis and fluorescence quenching, and the mRNA level of plastidic glutamine synthetase or of mitochondrial serine hydroxymethyltransferase (SHMT) in the leaves of the wild type and of the SHMT-deficient 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    Becker, T.W.7
  • 2
    • 0027300803 scopus 로고
    • Effects of tetrahydrofolate polyglutamates on the kinetic parameters of serine hydroxymethyltransferase and glycine decarboxylase from pea leaf mitochondria
    • Besson V. Rebeille F. Neuburger M. Douce R. Cossins E.A. 1993 Effects of tetrahydrofolate polyglutamates on the kinetic parameters of serine hydroxymethyltransferase and glycine decarboxylase from pea leaf mitochondria Biochem. J. 292 425 430
    • (1993) Biochem. J. , vol.292 , pp. 425-430
    • Besson, V.1    Rebeille, F.2    Neuburger, M.3    Douce, R.4    Cossins, E.A.5
  • 3
    • 0029200019 scopus 로고
    • Evidence for three serine hydroxymethyltransferases in green leaf cells: Purification and characterization of the mitochondrial and chloroplastic isoforms
    • Besson V. Neuburger M. Rebeille F. Douce R. 1995 Evidence for three serine hydroxymethyltransferases in green leaf cells: purification and characterization of the mitochondrial and chloroplastic isoforms Plant Physiol. Biochem. 33 665 673
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 665-673
    • Besson, V.1    Neuburger, M.2    Rebeille, F.3    Douce, R.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0001161928 scopus 로고
    • Immunological studies on glutamine synthetase using antisera raised to the two plant forms of the enzyme from Phaseolus root nodules
    • Cullimore J.V. Miflin B.J. 1974 Immunological studies on glutamine synthetase using antisera raised to the two plant forms of the enzyme from Phaseolus root nodules J. Exp. Bot. 35 581 587
    • (1974) J. Exp. Bot. , vol.35 , pp. 581-587
    • Cullimore, J.V.1    Miflin, B.J.2
  • 6
    • 0024286729 scopus 로고
    • Determination of ammonium ion by fluorometry after on-line derivatization with o-phthaldialdehyde
    • Goyal S.S. Rains D.W. Huffaker R.C. 1988 Determination of ammonium ion by fluorometry after on-line derivatization with o-phthaldialdehyde Anal. Chem. 60 175 179
    • (1988) Anal. Chem. , vol.60 , pp. 175-179
    • Goyal, S.S.1    Rains, D.W.2    Huffaker, R.C.3
  • 9
    • 0035037362 scopus 로고    scopus 로고
    • Metabolic response of potato plants to an antisense reduction of the P-protein of glycine decarboxylase
    • Heineke D. Bykova N. Gardeström P. Bauwe H. 2001 Metabolic response of potato plants to an antisense reduction of the P-protein of glycine decarboxylase Planta 212 880 887
    • (2001) Planta , vol.212 , pp. 880-887
    • Heineke, D.1    Bykova, N.2    Gardeström, P.3    Bauwe, H.4
  • 10
    • 0034095789 scopus 로고    scopus 로고
    • A critical experimental evaluation of methods for determination of NH
    • in plant tissue, xylem sap and apoplastic fluid
    • Husted S. Hebbern C.A. Mattsson M. Schjoerring J.K. 2000 A critical experimental evaluation of methods for determination of NH in plant tissue, xylem sap and apoplastic fluid Physiol. Plant. 109 167 179
    • (2000) Physiol. Plant. , vol.109 , pp. 167-179
    • Husted, S.1    Hebbern, C.A.2    Mattsson, M.3    Schjoerring, J.K.4
  • 11
    • 0032940292 scopus 로고    scopus 로고
    • Nitrate reductase in higher plants: A case study for transduction of environmental stimuli into control of activity
    • Kaiser W.M. Weiner H. Huber S.C. 1999 Nitrate reductase in higher plants: a case study for transduction of environmental stimuli into control of activity Physiol. Plant. 105 385 390
    • (1999) Physiol. Plant. , vol.105 , pp. 385-390
    • Kaiser, W.M.1    Weiner, H.2    Huber, S.C.3
  • 13
    • 0029193207 scopus 로고
    • Serine hydroxymethyltransferase from Solanum tuberosum
    • Kopriva S. Bauwe H. 1995 Serine hydroxymethyltransferase from Solanum tuberosum Plant Physiol. 107 271 272
    • (1995) Plant Physiol. , vol.107 , pp. 271-272
    • Kopriva, S.1    Bauwe, H.2
  • 14
    • 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
  • 16
    • 0032068626 scopus 로고    scopus 로고
    • Glutamine synthetase isoenzymes, oligomers and subunits from hairy roots of Beta vulgaris L. var. lutea
    • Mäck G. 1998 Glutamine synthetase isoenzymes, oligomers and subunits from hairy roots of Beta vulgaris L. var. lutea Planta 205 113 120
    • (1998) Planta , vol.205 , pp. 113-120
    • MäcK, G.1
  • 17
    • 0035170619 scopus 로고    scopus 로고
    • Elevated carbon dioxide increases nitrate uptake and nitrate reductase activity when tobacco is growing on nitrate, but increases ammonium uptake and inhibits nitrate reductase activity when tobacco is growing on ammonium nitrate
    • Matt P. Geiger M. Walch-Liu P. Engels C. Krapp A. Stitt M. 2001 Elevated carbon dioxide increases nitrate uptake and nitrate reductase activity when tobacco is growing on nitrate, but increases ammonium uptake and inhibits nitrate reductase activity when tobacco is growing on ammonium nitrate Plant Cell Environ. 24 1119 1137
    • (2001) Plant Cell Environ. , vol.24 , pp. 1119-1137
    • Matt, P.1    Geiger, M.2    Walch-Liu, P.3    Engels, C.4    Krapp, A.5    Stitt, M.6
  • 18
    • 17544365664 scopus 로고    scopus 로고
    • Ammonia emission from young barley plants: Influence of N source, light/dark cycles and inhibition of glutamine synthetase
    • Mattsson M. Schjoerring J.K. 1996 Ammonia emission from young barley plants: influence of N source, light/dark cycles and inhibition of glutamine synthetase J. Exp. Bot. 47 477 484
    • (1996) J. Exp. Bot. , vol.47 , pp. 477-484
    • Mattsson, M.1    Schjoerring, J.K.2
  • 20
    • 0034029208 scopus 로고    scopus 로고
    • Integrated temporal regulation of the photorespiratory pathway. Circadian regulation of two Arabidopsis genes encoding serine hydroxymethyltransferase
    • McClung C.R. Hsu M. Painter J.E. Gagne J.M. Karlsberg S.D. Salomé P.A. 2000 Integrated temporal regulation of the photorespiratory pathway. Circadian regulation of two Arabidopsis genes encoding serine hydroxymethyltransferase Plant Physiol. 123 381 391
    • (2000) Plant Physiol. , vol.123 , pp. 381-391
    • McClung, C.R.1    Hsu, M.2    Painter, J.E.3    Gagne, J.M.4    Karlsberg, S.D.5    Salomé, P.A.6
  • 21
    • 0030741035 scopus 로고    scopus 로고
    • The expression of the tobacco genes encoding plastidic glutamine synthetase or ferredoxin-dependent glutamate synthase does not depend on the rate of nitrate reduction, and is unaffected by suppression of photorespiration
    • Migge A. Carrayol E. Kunz C. Hirel B. Fock H. Becker T.W. 1997 The expression of the tobacco genes encoding plastidic glutamine synthetase or ferredoxin-dependent glutamate synthase does not depend on the rate of nitrate reduction, and is unaffected by suppression of photorespiration J. Exp. Bot. 48 1175 1184
    • (1997) J. Exp. Bot. , vol.48 , pp. 1175-1184
    • Migge, A.1    Carrayol, E.2    Kunz, C.3    Hirel, B.4    Fock, H.5    Becker, T.W.6
  • 22
    • 13844261168 scopus 로고    scopus 로고
    • Arabidopsis SHMT1, a serine hydroxymethyltransferase that functions in the photorespiratory pathway influences resistance to biotic and abiotic stress
    • Moreno J.I. Martin R. Castrena C. 2005 Arabidopsis SHMT1, a serine hydroxymethyltransferase that functions in the photorespiratory pathway influences resistance to biotic and abiotic stress Plant J. 41 451 463
    • (2005) Plant J. , vol.41 , pp. 451-463
    • Moreno, J.I.1    Martin, R.2    Castrena, C.3
  • 23
    • 0002324424 scopus 로고
    • Asparagine synthetase in Zea mays
    • Oaks A. Ross D.W. 1984 Asparagine synthetase in Zea mays Can. J. Bot. 62 68 73
    • (1984) Can. J. Bot. , vol.62 , pp. 68-73
    • Oaks, A.1    Ross, D.W.2
  • 24
    • 33644871529 scopus 로고
    • Pea leaf glutamine synthetase-regulatory properties
    • O'Neal T.D. Joy K.W. 1975 Pea leaf glutamine synthetase-regulatory properties Plant Physiol. 55 968 974
    • (1975) Plant Physiol. , vol.55 , pp. 968-974
    • O'Neal, T.D.1    Joy, K.W.2
  • 25
    • 0029659032 scopus 로고    scopus 로고
    • 13C nuclear magnetic resonance detection of interaction of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboylase complex activities in Arabidopsis
    • 13C nuclear magnetic resonance detection of interaction of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboylase complex activities in Arabidopsis Plant Physiol. 112 207 216
    • (1996) Plant Physiol. , vol.112 , pp. 207-216
    • Prabhu, V.1    Chatson, K.B.2    Abrams, G.D.3    King, J.4
  • 26
    • 0026468562 scopus 로고
    • An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase
    • Richards N.G.J. Schuster S.M. 1992 An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase FEBS Lett. 313 98 102
    • (1992) FEBS Lett. , vol.313 , pp. 98-102
    • Richards, N.G.J.1    Schuster, S.M.2
  • 28
    • 0020005825 scopus 로고
    • Serine hydroxymethyltransferase
    • Schirch L. 1982 Serine hydroxymethyltransferase Adv. Enzymol. 53 83 112
    • (1982) Adv. Enzymol. , vol.53 , pp. 83-112
    • Schirch, L.1
  • 29
    • 0029360484 scopus 로고
    • Light dependent and tissue specific expression of the H-protein of the glycine decarboxylase complex
    • Srinivasan R. Oliver D.J. 1995 Light dependent and tissue specific expression of the H-protein of the glycine decarboxylase complex Plant Physiol. 109 161 168
    • (1995) Plant Physiol. , vol.109 , pp. 161-168
    • Srinivasan, R.1    Oliver, D.J.2
  • 30
    • 0000598063 scopus 로고
    • Analysis of cis-active sequences involved in the leaf-specific expression of a potato gene in transgenic plants
    • Stockhaus J. Eckes P. Rocha-Sosa M. Schell J. Willmitzer L. 1987 Analysis of cis-active sequences involved in the leaf-specific expression of a potato gene in transgenic plants Proc. Natl Acad. Sci. USA 84 7943 7947
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7943-7947
    • Stockhaus, J.1    Eckes, P.2    Rocha-Sosa, M.3    Schell, J.4    Willmitzer, L.5
  • 31
    • 0027947707 scopus 로고
    • Immunological characterization of ferredoxin and methylviologen interaction domains of glutamate synthase using monoclonal antibodies
    • Suzuki A. Vergnet C. Morot-Gaudry J.-F. Zehnacker C. Grosclaude J. 1994 Immunological characterization of ferredoxin and methylviologen interaction domains of glutamate synthase using monoclonal antibodies Plant Physiol. Biochem. 32 619 626
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 619-626
    • Suzuki, A.1    Vergnet, C.2    Morot-Gaudry, J.-F.3    Zehnacker, C.4    Grosclaude, J.5
  • 32
    • 0002167092 scopus 로고
    • Radioactive assay for serine transhydroxymethylase
    • Taylor R.T. Weissbach H. 1965 Radioactive assay for serine transhydroxymethylase Anal. Biochem. 13 80 84
    • (1965) Anal. Biochem. , vol.13 , pp. 80-84
    • Taylor, R.T.1    Weissbach, H.2
  • 33
    • 0025156795 scopus 로고
    • Dark-induced and organ-specific expression of two asparagine synthetase genes in Pisum sativum
    • Tsai F.-Y. Coruzzi G. 1990 Dark-induced and organ-specific expression of two asparagine synthetase genes in Pisum sativum EMBO J. 9 323 332
    • (1990) EMBO J. , vol.9 , pp. 323-332
    • Tsai, F.-Y.1    Coruzzi, G.2
  • 34
    • 0026766649 scopus 로고
    • Identification and localization of multiple forms of serine hydroxymethyltransferase in pea (Pisum sativum) and characterization of a cDNA encoding a mitochondrial isoform
    • Turner S.R. Ireland R. Morgan C. Rawsthorne S. 1992 Identification and localization of multiple forms of serine hydroxymethyltransferase in pea (Pisum sativum) and characterization of a cDNA encoding a mitochondrial isoform J. Biol. Chem. 267 13528 13534
    • (1992) J. Biol. Chem. , vol.267 , pp. 13528-13534
    • Turner, S.R.1    Ireland, R.2    Morgan, C.3    Rawsthorne, S.4
  • 35
    • 0031588714 scopus 로고    scopus 로고
    • Using quaternary high-performance liquid chromatography eluent systems for separating 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate-derivatized amino acid mixtures
    • Van Wandelen C. Cohen S.A. 1997 Using quaternary high-performance liquid chromatography eluent systems for separating 6-aminoquinolyl-N- hydroxysuccinimidyl-carbamate-derivatized amino acid mixtures J. Chromatogr. A 763 11 22
    • (1997) J. Chromatogr. a , vol.763 , pp. 11-22
    • Van Wandelen, C.1    Cohen, S.A.2
  • 36
    • 0001234970 scopus 로고
    • Barley mutants lacking chloroplast glutamine synthetase: Biochemical and genetic analysis
    • Wallsgrove R.M. Turner J.C. Hall N.P. Kendall A.C. Bright S.W.J. 1987 Barley mutants lacking chloroplast glutamine synthetase: biochemical and genetic analysis Plant Physiol. 83 155 158
    • (1987) Plant Physiol. , vol.83 , pp. 155-158
    • Wallsgrove, R.M.1    Turner, J.C.2    Hall, N.P.3    Kendall, A.C.4    Bright, S.W.J.5
  • 37
    • 0030916466 scopus 로고    scopus 로고
    • Control of photosynthesis in barley mutants with reduced activities of glycine decarboxylase
    • Wingler A. Lea P.J. Leegood R.C. 1997 Control of photosynthesis in barley mutants with reduced activities of glycine decarboxylase Planta 202 171 178
    • (1997) Planta , vol.202 , pp. 171-178
    • Wingler, A.1    Lea, P.J.2    Leegood, R.C.3
  • 38
    • 0032946768 scopus 로고    scopus 로고
    • The role of photorespiration during drought stress: An analysis utilising barley mutants with reduced activities of photorespiratory enzymes
    • Wingler A. Quick W.P. Bungard R.A. Bailey K.J. Lea P.J. Leegood R.C. 1999 The role of photorespiration during drought stress: an analysis utilising barley mutants with reduced activities of photorespiratory enzymes Plant Cell Environ. 22 361 373
    • (1999) Plant Cell Environ. , vol.22 , pp. 361-373
    • Wingler, A.1    Quick, W.P.2    Bungard, R.A.3    Bailey, K.J.4    Lea, P.J.5    Leegood, R.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.