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Volumn 219, Issue 1, 2004, Pages 59-65

Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in high nitrite excretion and NO emission from leaf and root tissue

Author keywords

Nicotiana; Nitrate reductase; Nitric oxide; Nitrite excretion; Phosphorylation

Indexed keywords

ENZYME KINETICS; MUTAGENESIS; NITRATES; ORGANIC ACIDS; TISSUE; TOBACCO;

EID: 2442624568     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-004-1209-6     Document Type: Article
Times cited : (89)

References (33)
  • 2
    • 0036007974 scopus 로고    scopus 로고
    • Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase
    • Athwal GS, Huber SC (2002) Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase. Plant J 29:119-129
    • (2002) Plant J , vol.29 , pp. 119-129
    • Athwal, G.S.1    Huber, S.C.2
  • 3
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
    • Bachmann M, Shiraishi N, Campbell WH, Yoo B-C, Harmon AC, Huber SC (1996) Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8:505-517
    • (1996) Plant Cell , vol.8 , pp. 505-517
    • Bachmann, M.1    Shiraishi, N.2    Campbell, W.H.3    Yoo, B.-C.4    Harmon, A.C.5    Huber, S.C.6
  • 4
    • 0030901601 scopus 로고    scopus 로고
    • Nitrate reductase activation state in barley roots in relation to the energy and carbohydrate status
    • Botrel A, Kaiser WM (1997) Nitrate reductase activation state in barley roots in relation to the energy and carbohydrate status. Planta 201:496-501
    • (1997) Planta , vol.201 , pp. 496-501
    • Botrel, A.1    Kaiser, W.M.2
  • 5
    • 0029847671 scopus 로고    scopus 로고
    • Nitrate reduction, nitrite reduction and ammonia assimilation in barley roots in response to anoxia
    • Botrel A, Magné C, Kaiser WM (1996) Nitrate reduction, nitrite reduction and ammonia assimilation in barley roots in response to anoxia. Plant Physiol Biochem 34:645-652
    • (1996) Plant Physiol Biochem , vol.34 , pp. 645-652
    • Botrel, A.1    Magné, C.2    Kaiser, W.M.3
  • 6
    • 0141678892 scopus 로고    scopus 로고
    • Expression of a stress-induced hemoglobin affects NO levels produced by alfalfa root cultures under hypoxic stress
    • Dordas C, Hasinoff BB, Igamberdiev AU, Manac'h N, Rivoal J, Hill RD (2003) Expression of a stress-induced hemoglobin affects NO levels produced by alfalfa root cultures under hypoxic stress. Plant J 35:763-770
    • (2003) Plant J , vol.35 , pp. 763-770
    • Dordas, C.1    Hasinoff, B.B.2    Igamberdiev, A.U.3    Manac'h, N.4    Rivoal, J.5    Hill, R.D.6
  • 7
    • 0029583746 scopus 로고
    • Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves
    • Douglas P, Morrice N, MacKintosh C (1995) Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves. FEBS Lett 377:113-117
    • (1995) FEBS Lett , vol.377 , pp. 113-117
    • Douglas, P.1    Morrice, N.2    MacKintosh, C.3
  • 8
    • 0345228268 scopus 로고
    • Role of ATP in nitrite reduction in roots of wheat and pea
    • Dry I, Wallace W, Nicholas DJD (1981) Role of ATP in nitrite reduction in roots of wheat and pea. Planta 152:234-238
    • (1981) Planta , vol.152 , pp. 234-238
    • Dry, I.1    Wallace, W.2    Nicholas, D.J.D.3
  • 9
    • 0001145102 scopus 로고
    • Anaerobic nitrite production by plant cells and tissues: Evidence for two nitrate pools
    • Ferrari TE, Yoder OC, Filner P (1973) Anaerobic nitrite production by plant cells and tissues: evidence for two nitrate pools. Plant Physiol 51:423-431
    • (1973) Plant Physiol , vol.51 , pp. 423-431
    • Ferrari, T.E.1    Yoder, O.C.2    Filner, P.3
  • 10
    • 0036914587 scopus 로고    scopus 로고
    • Metabolic enzymes as targets for 14-3-3 proteins
    • Huber SC, MacKintosh C, Kaiser WM (2002) Metabolic enzymes as targets for 14-3-3 proteins. Plant Mol Biol 50:1053-1063
    • (2002) Plant Mol Biol , vol.50 , pp. 1053-1063
    • Huber, S.C.1    MacKintosh, C.2    Kaiser, W.M.3
  • 11
    • 0034060414 scopus 로고    scopus 로고
    • Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase in leaf extracts: What limits nitrate reduction in situ?
    • Kaiser WM, Kandlbinder A, Stoimenova M, Glaab J (2000) Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase in leaf extracts: What limits nitrate reduction in situ? Planta 210:801-807
    • (2000) Planta , vol.210 , pp. 801-807
    • Kaiser, W.M.1    Kandlbinder, A.2    Stoimenova, M.3    Glaab, J.4
  • 12
    • 2442553843 scopus 로고    scopus 로고
    • Modulation of nitrate reductase activity and (eco)physiological implications
    • Stulen I, Amancio Z (eds) chapter 7. Kluwer, Dordrecht
    • Kaiser WM, Planchet E, Stoimenova M, Sonoda M (2004) Modulation of nitrate reductase activity and (eco)physiological implications. In: Stulen I, Amancio Z (eds) N metabolism and plant adaption to the environment, chapter 7. Kluwer, Dordrecht
    • (2004) N Metabolism and Plant Adaption to the Environment
    • Kaiser, W.M.1    Planchet, E.2    Stoimenova, M.3    Sonoda, M.4
  • 13
    • 0002757067 scopus 로고
    • The release of nitrite from barley roots in response to metabolic inhibitors, uncoupling agents and anoxia
    • Lee RB (1979) The release of nitrite from barley roots in response to metabolic inhibitors, uncoupling agents and anoxia. J Exp Bot 30:119-133
    • (1979) J Exp Bot , vol.30 , pp. 119-133
    • Lee, R.B.1
  • 14
    • 0034787902 scopus 로고    scopus 로고
    • Retrotransposons of the Tnt1B family are mobile in Nicotiana plumbaginifolia and can induce alternative splicing of the host gene upon insertion
    • Leprince A-S, Grandbastien M-A, Meyer C (2001) Retrotransposons of the Tnt1B family are mobile in Nicotiana plumbaginifolia and can induce alternative splicing of the host gene upon insertion. Plant Mol Biol 47:533-541
    • (2001) Plant Mol Biol , vol.47 , pp. 533-541
    • Leprince, A.-S.1    Grandbastien, M.-A.2    Meyer, C.3
  • 15
    • 2442614911 scopus 로고    scopus 로고
    • Light regulation of nitrate uptake, assimilation and metabolism
    • Stulen I, Amancio Z (eds) chapter 6. Kluwer, Dordrecht
    • Lillo C (2004) Light regulation of nitrate uptake, assimilation and metabolism. In: Stulen I, Amancio Z (eds) N metabolism and plant adaption to the environment, chapter 6. Kluwer, Dordrecht
    • (2004) N Metabolism and Plant Adaption to the Environment
    • Lillo, C.1
  • 16
    • 84989692631 scopus 로고
    • Comparative studies of diurnal variations of nitrate reductase activity in wheat, oat and barley
    • Lillo C, Henriksen A (1984) Comparative studies of diurnal variations of nitrate reductase activity in wheat, oat and barley. Physiol Plant 62:89-94
    • (1984) Physiol Plant , vol.62 , pp. 89-94
    • Lillo, C.1    Henriksen, A.2
  • 17
    • 0031397707 scopus 로고    scopus 로고
    • Characterization of nitrate reductase from light- and dark-exposed leaves
    • Lillo C, Kazaic S, Ruoff P, Meyer C (1997) Characterization of nitrate reductase from light- and dark-exposed leaves. Plant Physiol 114:1377-1383
    • (1997) Plant Physiol , vol.114 , pp. 1377-1383
    • Lillo, C.1    Kazaic, S.2    Ruoff, P.3    Meyer, C.4
  • 18
    • 0141458090 scopus 로고    scopus 로고
    • Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in constitutive activation of the enzyme in vivo and nitrite accumulation
    • Lillo C, Lea US, Leydecker M-T, Meyer C (2003) Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in constitutive activation of the enzyme in vivo and nitrite accumulation. Plant J 35:566-573
    • (2003) Plant J , vol.35 , pp. 566-573
    • Lillo, C.1    Lea, U.S.2    Leydecker, M.-T.3    Meyer, C.4
  • 19
    • 0040949996 scopus 로고
    • Effect of aerobic and anaerobic conditions on the in vivo nitrate reductase assay in spinach leaves
    • Mann AF, Hucklesby DP, Hewitt EJ (1979) Effect of aerobic and anaerobic conditions on the in vivo nitrate reductase assay in spinach leaves. Planta 146:83-89
    • (1979) Planta , vol.146 , pp. 83-89
    • Mann, A.F.1    Hucklesby, D.P.2    Hewitt, E.J.3
  • 20
    • 0000050273 scopus 로고
    • Vacuoles as storage compartment for nitrate in barley leaves
    • Martinoia E, Heck U, Wiemken A (1981) Vacuoles as storage compartment for nitrate in barley leaves. Nature 289:292-294
    • (1981) Nature , vol.289 , pp. 292-294
    • Martinoia, E.1    Heck, U.2    Wiemken, A.3
  • 21
    • 0002987694 scopus 로고    scopus 로고
    • Nitrate reduction and signalling
    • Lea PJ, Morot-Gaudry JF (eds) Springer, Berlin Heidelberg New York
    • Meyer C, Stitt M (2001) Nitrate reduction and signalling. In: Lea PJ, Morot-Gaudry JF (eds) Plant nitrogen. Springer, Berlin Heidelberg New York, pp 37-59
    • (2001) Plant Nitrogen , pp. 37-59
    • Meyer, C.1    Stitt, M.2
  • 23
    • 0034124525 scopus 로고    scopus 로고
    • Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties
    • Provan F, Aksland L-M, Meyer C, Lillo C (2000) Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties. Plant Physiol 123:757-764
    • (2000) Plant Physiol , vol.123 , pp. 757-764
    • Provan, F.1    Aksland, L.-M.2    Meyer, C.3    Lillo, C.4
  • 24
    • 0001609854 scopus 로고
    • Decrease of nitrate reductase activity in spinach leaves during a light-dark transition
    • Riens B, Heldt HW (1992) Decrease of nitrate reductase activity in spinach leaves during a light-dark transition. Plant Physiol 98:573-577
    • (1992) Plant Physiol , vol.98 , pp. 573-577
    • Riens, B.1    Heldt, H.W.2
  • 25
    • 0036006867 scopus 로고    scopus 로고
    • Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro
    • Rockel P, Strube F, Rockel A, Wildt J, Kaiser WM (2002) Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro. J Exp Bot 53:103-110
    • (2002) J Exp Bot , vol.53 , pp. 103-110
    • Rockel, P.1    Strube, F.2    Rockel, A.3    Wildt, J.4    Kaiser, W.M.5
  • 26
    • 0025222742 scopus 로고
    • Molecular oxygen as electron acceptor in the NADH-nitrate reductase system
    • Ruoff P, Lillo C (1990) Molecular oxygen as electron acceptor in the NADH-nitrate reductase system. Biochem Biophys Res Commun 172:1000-1005
    • (1990) Biochem Biophys Res Commun , vol.172 , pp. 1000-1005
    • Ruoff, P.1    Lillo, C.2
  • 27
    • 0001669390 scopus 로고
    • On the regulation of spinach nitrate reductase
    • Sanchez J, Heldt HW (1990) On the regulation of spinach nitrate reductase. Plant Physiol 92:684-689
    • (1990) Plant Physiol , vol.92 , pp. 684-689
    • Sanchez, J.1    Heldt, H.W.2
  • 28
    • 0041346391 scopus 로고    scopus 로고
    • The role of nitrate reduction in the anoxic metabolism of roots. I. Characterization of root morphology and normoxic metabolism of wild type tobacco and a transformant lacking root nitrate reductase
    • Stoimenova M, Hänsch R, Mendel R, Gimmler H, Kaiser WM (2003a) The role of nitrate reduction in the anoxic metabolism of roots. I. Characterization of root morphology and normoxic metabolism of wild type tobacco and a transformant lacking root nitrate reductase. Plant Soil 253:145-153
    • (2003) Plant Soil , vol.253 , pp. 145-153
    • Stoimenova, M.1    Hänsch, R.2    Mendel, R.3    Gimmler, H.4    Kaiser, W.M.5
  • 29
    • 0041346389 scopus 로고    scopus 로고
    • The role of nitrate reduction in the anoxic metabolism of roots. II. Anoxic metabolism of tobacco roots with or without nitrate reductase activity
    • Stoimenova M, Liboureligl, Ratcliffe RG, Kaiser WM (2003b) The role of nitrate reduction in the anoxic metabolism of roots. II. Anoxic metabolism of tobacco roots with or without nitrate reductase activity. Plant Soil 253:155-167
    • (2003) Plant Soil , vol.253 , pp. 155-167
    • Stoimenova, M.1    Liboureligl2    Ratcliffe, R.G.3    Kaiser, W.M.4
  • 30
    • 0030095876 scopus 로고    scopus 로고
    • Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase
    • Su W, Huber SC, Crawford NM (1996) Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell 8:519-527
    • (1996) Plant Cell , vol.8 , pp. 519-527
    • Su, W.1    Huber, S.C.2    Crawford, N.M.3
  • 31
    • 0031924865 scopus 로고    scopus 로고
    • Remobilisation of vacuolar stored nitrate in barley root cells
    • van der Leij M, Smith SJ, Miller AJ (1998) Remobilisation of vacuolar stored nitrate in barley root cells. Planta 205:64-72
    • (1998) Planta , vol.205 , pp. 64-72
    • Van Der Leij, M.1    Smith, S.J.2    Miller, A.J.3
  • 32
    • 0025735599 scopus 로고
    • Constitutive expression of nitrate reductase allows normal growth and development of Nicotiana plumbaginifolia plants
    • Vincentz M, Caboche M (1991) Constitutive expression of nitrate reductase allows normal growth and development of Nicotiana plumbaginifolia plants EMBO J 10:1027-1035
    • (1991) EMBO J , vol.10 , pp. 1027-1035
    • Vincentz, M.1    Caboche, M.2
  • 33
    • 0033952545 scopus 로고    scopus 로고
    • Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: In vitro evidence for the NR-dependent formation of active nitrogen species
    • Yamasaki H, Sakihama Y (2000) Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species. FEBS Lett 468:89-92
    • (2000) FEBS Lett , vol.468 , pp. 89-92
    • Yamasaki, H.1    Sakihama, Y.2


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