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Volumn 115, Issue 3, 1997, Pages 1135-1143

Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; ALANINE; ARABIDOPSIS; CYSTEINE; ENZYME ACTIVITY; ENZYME PURIFICATION; HOMOGENEITY; INCUBATION; MUTANT; NICOTINAMIDE ADENINE DEHYDROGENASE; NITRATE REDUCTASE; RESIDUE; SERINE; TARGETED MUTAGENESIS;

EID: 0031277446     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.115.3.1135     Document Type: Article
Times cited : (33)

References (48)
  • 1
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor of phosphorylated nitrate reductase from spinach is a 14-3-3 protein
    • Bachmann M, Huber JL, Liao P-C, Gage DA, Huber SC (1996a) The inhibitor of phosphorylated nitrate reductase from spinach is a 14-3-3 protein. FEBS Lett 387: 127-131
    • (1996) FEBS Lett , vol.387 , pp. 127-131
    • Bachmann, M.1    Huber, J.L.2    Liao, P.-C.3    Gage, D.A.4    Huber, S.C.5
  • 2
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-543 as the major regula- Tory phosphorylation site in spinach leaf nitrate reductase
    • Bachmann M, Shiraishi N, Campbell WH, Yoo BC, Harmon AC, Huber SC (1996b) Identification of Ser-543 as the major regula- tory 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
  • 3
    • 0025696447 scopus 로고
    • A conserved cysteine in molybdenum oxotransferases
    • Barber MJ, Neame PJ (1990) A conserved cysteine in molybdenum oxotransferases. J Biol Chem 265: 20912-20915
    • (1990) J Biol Chem , vol.265 , pp. 20912-20915
    • Barber, M.J.1    Neame, P.J.2
  • 4
    • 0001398971 scopus 로고
    • Spinach nitrate reductase. Effects of ionic strength and pH on the full and partial enzyme activities
    • Barber MJ, Notton BA (1990) Spinach nitrate reductase. Effects of ionic strength and pH on the full and partial enzyme activities. Plant Physiol 93: 537-540
    • (1990) Plant Physiol , vol.93 , pp. 537-540
    • Barber, M.J.1    Notton, B.A.2
  • 5
    • 0025974216 scopus 로고
    • High efficiency of transformation of yeast by electroproration
    • Becker DM, Guarente L (1990) High efficiency of transformation of yeast by electroproration. Methods Enzymol 194: 182
    • (1990) Methods Enzymol , vol.194 , pp. 182
    • Becker, D.M.1    Guarente, L.2
  • 7
    • 0000788444 scopus 로고
    • Expression in Escherichia coli of cytochrome c reductase activity from a maize NADH:nitrate reductase complementary DNA
    • Campbell WH (1991) Expression in Escherichia coli of cytochrome c reductase activity from a maize NADH:nitrate reductase complementary DNA. Plant Physiol 99: 693-699
    • (1991) Plant Physiol , vol.99 , pp. 693-699
    • Campbell, W.H.1
  • 8
    • 0000324745 scopus 로고    scopus 로고
    • Nitrate reductase biochemistry comes of age
    • Campbell WH (1996) Nitrate reductase biochemistry comes of age. Plant Physiol 111: 355-361
    • (1996) Plant Physiol , vol.111 , pp. 355-361
    • Campbell, W.H.1
  • 9
    • 0025367363 scopus 로고
    • Functional domains of assimilatory nitrate reductases and nitrite reductases
    • Campbell WH, Kinghorn JR (1990) Functional domains of assimilatory nitrate reductases and nitrite reductases. Trends Biochem Sci 15: 315-319
    • (1990) Trends Biochem Sci , vol.15 , pp. 315-319
    • Campbell, W.H.1    Kinghorn, J.R.2
  • 10
    • 0000094361 scopus 로고
    • Purification and kinetics of higher plant NADH:nitrate reductase
    • Campbell WH, Smarrelli J (1978) Purification and kinetics of higher plant NADH:nitrate reductase. Plant Physiol 61: 611-616
    • (1978) Plant Physiol , vol.61 , pp. 611-616
    • Campbell, W.H.1    Smarrelli, J.2
  • 11
    • 0027535120 scopus 로고
    • Expression and characterization of the heme-binding domain of Chlorella nitrate reductase
    • Cannons AC, Barber MJ, Solomonson LP (1993) Expression and characterization of the heme-binding domain of Chlorella nitrate reductase. J Biol Chem 268: 3268-3271
    • (1993) J Biol Chem , vol.268 , pp. 3268-3271
    • Cannons, A.C.1    Barber, M.J.2    Solomonson, L.P.3
  • 12
    • 0029328453 scopus 로고
    • Nitrate: Nutrient and signal for plant growth
    • Crawford NM (1995) Nitrate: nutrient and signal for plant growth. Plant Cell 7: 859-868
    • (1995) Plant Cell , vol.7 , pp. 859-868
    • Crawford, N.M.1
  • 13
    • 0027144985 scopus 로고
    • The molecular genetics of nitrate assimilation in fungi and plants
    • Crawford NM, Arst HN (1993) The molecular genetics of nitrate assimilation in fungi and plants. Annu Rev Genet 27: 115-146
    • (1993) Annu Rev Genet , vol.27 , pp. 115-146
    • Crawford, N.M.1    Arst, H.N.2
  • 14
    • 0024039650 scopus 로고
    • Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains
    • Crawford NM, Smith M, Bellissimo D, Davis RW (1988) Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains. Proc Natl Acad Sci USA 85: 5006-5010
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5006-5010
    • Crawford, N.M.1    Smith, M.2    Bellissimo, D.3    Davis, R.W.4
  • 15
    • 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 P, 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, P.2    MacKintosh, C.3
  • 16
    • 0028174282 scopus 로고
    • Identification of an "essential" cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain
    • Dwivedi UN, Shiraishi N, Campbell WH (1994) Identification of an "essential" cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain. J Biol.Chem 269: 13785-13791
    • (1994) J Biol.Chem , vol.269 , pp. 13785-13791
    • Dwivedi, U.N.1    Shiraishi, N.2    Campbell, W.H.3
  • 17
    • 0028918858 scopus 로고
    • Site-directed mutagenesis of nitrate reductase from Aspergillus nidulans
    • Garde J, Kinghorn JR, Tomsett AB (1995) Site-directed mutagenesis of nitrate reductase from Aspergillus nidulans. J Biol Chem 270: 6644-6650
    • (1995) J Biol Chem , vol.270 , pp. 6644-6650
    • Garde, J.1    Kinghorn, J.R.2    Tomsett, A.B.3
  • 18
    • 0028140249 scopus 로고
    • Molecular cloning of rat liver sulfite oxidase
    • Garrett RM, Rajagopalan KV (1994) Molecular cloning of rat liver sulfite oxidase. J Biol Chem 269: 272-276
    • (1994) J Biol Chem , vol.269 , pp. 272-276
    • Garrett, R.M.1    Rajagopalan, K.V.2
  • 19
    • 0029876533 scopus 로고    scopus 로고
    • Site-directed mutagenesis of recombinant sulfite oxidase
    • Garrett RM, Rajagopalan KV (1996) Site-directed mutagenesis of recombinant sulfite oxidase. J Biol Chem 271: 7387-7391
    • (1996) J Biol Chem , vol.271 , pp. 7387-7391
    • Garrett, R.M.1    Rajagopalan, K.V.2
  • 20
    • 0029609221 scopus 로고
    • Functional analysis by site-directed mutagenesis of individual amino acid residues in the flavin domain of Neurospora crassa nitrate reductase
    • Gonzalez C, Brito N, Marzluf GA (1995) Functional analysis by site-directed mutagenesis of individual amino acid residues in the flavin domain of Neurospora crassa nitrate reductase. Mol Gen Genet 249: 456-464
    • (1995) Mol Gen Genet , vol.249 , pp. 456-464
    • Gonzalez, C.1    Brito, N.2    Marzluf, G.A.3
  • 21
    • 0025928680 scopus 로고
    • Production of recombinant proteins in the methylotrophic yeast Pichia pastoris
    • R Seetharam, SK Sharma, eds, Marcel Dekker, New York
    • Hagenson MJS (1991) Production of recombinant proteins in the methylotrophic yeast Pichia pastoris. In R Seetharam, SK Sharma, eds, Purification and Analysis of Recombinant Proteins. Marcel Dekker, New York, pp 193-212
    • (1991) Purification and Analysis of Recombinant Proteins , pp. 193-212
    • Hagenson, M.J.S.1
  • 22
    • 0001823786 scopus 로고
    • Recombinant PCR
    • MA Innis, DH Gelfand, JJ Sninsky, TJ White, eds, Academic Press, San Diego, CA
    • Higuchi R (1990) Recombinant PCR. In MA Innis, DH Gelfand, JJ Sninsky, TJ White, eds, PCR Protocols: A Guide to Method and Application. Academic Press, San Diego, CA, pp 177-183
    • (1990) PCR Protocols: A Guide to Method and Application , pp. 177-183
    • Higuchi, R.1
  • 23
    • 85032070731 scopus 로고
    • The use of mutants and transgenic plants to study nitrate assimilation
    • Hoff JL, Truong HN, Caboche M (1994) The use of mutants and transgenic plants to study nitrate assimilation. Plant Cell Environ 17: 489-506
    • (1994) Plant Cell Environ , vol.17 , pp. 489-506
    • Hoff, J.L.1    Truong, H.N.2    Caboche, M.3
  • 24
    • 0026633177 scopus 로고
    • Reversible light dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation
    • Huber JL, Huber SC, Campbell WH, Redinbaugh MG (1992) Reversible light dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation, Arch Biochem Biophys 296: 58-65
    • (1992) Arch Biochem Biophys , vol.296 , pp. 58-65
    • Huber, J.L.1    Huber, S.C.2    Campbell, W.H.3    Redinbaugh, M.G.4
  • 26
    • 0025367107 scopus 로고
    • High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH: Cytochrome b5 reductase
    • Hyde GE, Campbell WH (1990) High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH: cytochrome b5 reductase. Biochem Biophys Res Commun 168: 1285-1291
    • (1990) Biochem Biophys Res Commun , vol.168 , pp. 1285-1291
    • Hyde, G.E.1    Campbell, W.H.2
  • 27
    • 0024717889 scopus 로고
    • Monoclonal antibody-based immunoaffinity chromatography for purifying corn and squash NADH:nitrate reductase. Evidence for an interchain disulfide bond in nitrate reductase
    • Hyde GE, Wilberding JA, Meyer AL, Campbell ER, Campbell WH (1989) Monoclonal antibody-based immunoaffinity chromatography for purifying corn and squash NADH:nitrate reductase. Evidence for an interchain disulfide bond in nitrate reductase. Plant Mol Biol 13: 233-246
    • (1989) Plant Mol Biol , vol.13 , pp. 233-246
    • Hyde, G.E.1    Wilberding, J.A.2    Meyer, A.L.3    Campbell, E.R.4    Campbell, W.H.5
  • 28
    • 0028317624 scopus 로고
    • Posttranslational regulation of nitrate reductase in higher plants
    • Kaiser WM, Huber SC (1994) Posttranslational regulation of nitrate reductase in higher plants. Plant Physiol 106: 817-821
    • (1994) Plant Physiol , vol.106 , pp. 817-821
    • Kaiser, W.M.1    Huber, S.C.2
  • 29
    • 84941084844 scopus 로고
    • Advances in nitrate assimilation
    • BJ Miflin, PJ Lea, eds, Academic Press, San Diego, CA
    • Kleinhofs A, Warner RL (1990) Advances in nitrate assimilation. In BJ Miflin, PJ Lea, eds, The Biochemistry of Plants. Academic Press, San Diego, CA, pp 89-120
    • (1990) The Biochemistry of Plants , pp. 89-120
    • Kleinhofs, A.1    Warner, R.L.2
  • 30
    • 0028225390 scopus 로고
    • A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis
    • Labrie ST, Crawford NM (1994) A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis. J Biol Chem 269: 14497-14501
    • (1994) J Biol Chem , vol.269 , pp. 14497-14501
    • Labrie, S.T.1    Crawford, N.M.2
  • 31
    • 0028774181 scopus 로고
    • Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 Å resolution: Relationship to other flavoprotein reductases
    • Lu G, Campbell WH, Schneider G, Lindqvist Y (1994) Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 Å resolution: relationship to other flavoprotein reductases. Structure 2: 809-821
    • (1994) Structure , vol.2 , pp. 809-821
    • Lu, G.1    Campbell, W.H.2    Schneider, G.3    Lindqvist, Y.4
  • 32
    • 0029075043 scopus 로고
    • Structural studies on corn nitrate reductase: Refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active site mutant and modeling of the cytochrome b domain
    • Lu G, Lindqvist Y, Schneider G, Dwivedi UN, Campbell WH (1995) Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active site mutant and modeling of the cytochrome b domain. J Mol Biol 248: 931-948
    • (1995) J Mol Biol , vol.248 , pp. 931-948
    • Lu, G.1    Lindqvist, Y.2    Schneider, G.3    Dwivedi, U.N.4    Campbell, W.H.5
  • 33
    • 0026768507 scopus 로고
    • Regulation of spinach-leaf nitrate reductase by reversible phosphorylation
    • Mackintosh C (1992) Regulation of spinach-leaf nitrate reductase by reversible phosphorylation. Biochim Biophys Acta 1137: 121-126
    • (1992) Biochim Biophys Acta , vol.1137 , pp. 121-126
    • Mackintosh, C.1
  • 34
    • 0025757379 scopus 로고
    • Mutational and structural analysis of the nitrate reductase heme domain of Nicotiana plumbaginifolia
    • Meyer C, Levin JM, Roussel JM, Rouze P (1991) Mutational and structural analysis of the nitrate reductase heme domain of Nicotiana plumbaginifolia. J Biol Chem 266: 20561-20566
    • (1991) J Biol Chem , vol.266 , pp. 20561-20566
    • Meyer, C.1    Levin, J.M.2    Roussel, J.M.3    Rouze, P.4
  • 35
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
    • Moorhead G, Douglas P, Morrice N, Scarable M, Aitken A, MacKintosh C (1996) Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr Biol 6: 1104-1113
    • (1996) Curr Biol , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarable, M.4    Aitken, A.5    MacKintosh, C.6
  • 36
    • 0030062088 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:nitrate reductase
    • Quinn GB, Trimboli AJ, Prosser IM, Barber MJ (1996) Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:nitrate reductase. Arch Biochem Biophys 327: 151-160
    • (1996) Arch Biochem Biophys , vol.327 , pp. 151-160
    • Quinn, G.B.1    Trimboli, A.J.2    Prosser, I.M.3    Barber, M.J.4
  • 37
    • 0028863485 scopus 로고
    • Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase
    • Ratnam K, Shiraishi N, Campbell WH, Mille R (1995) Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase. J Biol Chem 270: 24067-24072
    • (1995) J Biol Chem , vol.270 , pp. 24067-24072
    • Ratnam, K.1    Shiraishi, N.2    Campbell, W.H.3    Mille, R.4
  • 38
    • 0022431977 scopus 로고
    • Quaternary structure and composition of squash NADH:nitrate reductase
    • Redinbaugh MG, Campbell WH (1985) Quaternary structure and composition of squash NADH:nitrate reductase. J Biol Chem 260: 3380-3385
    • (1985) J Biol Chem , vol.260 , pp. 3380-3385
    • Redinbaugh, M.G.1    Campbell, W.H.2
  • 40
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC (1996) Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science 272: 1615-1620
    • (1996) Science , vol.272 , pp. 1615-1620
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 41
    • 0342882548 scopus 로고    scopus 로고
    • Expression of nitrate reductase FAD-containing fragments in Pichia
    • KJ Stevenson, ed, University of Calgary Press, Calgary, Alberta, Canada
    • Shiraishi N, Campbell WH (1997) Expression of nitrate reductase FAD-containing fragments in Pichia. In KJ Stevenson, ed, Flavins and Flavoproteins. University of Calgary Press, Calgary, Alberta, Canada, pp 931-934
    • (1997) Flavins and Flavoproteins , pp. 931-934
    • Shiraishi, N.1    Campbell, W.H.2
  • 43
    • 0016768222 scopus 로고
    • Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris
    • Solomonson LP, Lorimer GH, Hall RL, Borchers R, Bailey JL (1975) Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. J Biol Chem 250: 4120-4127
    • (1975) J Biol Chem , vol.250 , pp. 4120-4127
    • Solomonson, L.P.1    Lorimer, G.H.2    Hall, R.L.3    Borchers, R.4    Bailey, J.L.5
  • 44
    • 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
  • 45
    • 0025870851 scopus 로고
    • Characterization of Nicotiana tabacum nitrate reductase protein produced in Saccharomyces cerevisiae
    • Truong FN, Meyer C, Daniel-Vedele F (1991) Characterization of Nicotiana tabacum nitrate reductase protein produced in Saccharomyces cerevisiae. Biochem J 278: 393-397
    • (1991) Biochem J , vol.278 , pp. 393-397
    • Truong, F.N.1    Meyer, C.2    Daniel-Vedele, F.3
  • 46
    • 84983386932 scopus 로고
    • Genetics and molecular biology of nitrate metabolism
    • Warner RL, Kleinhofs A (1992) Genetics and molecular biology of nitrate metabolism. Physiol Plant 85: 245-252
    • (1992) Physiol Plant , vol.85 , pp. 245-252
    • Warner, R.L.1    Kleinhofs, A.2
  • 47
    • 0026150937 scopus 로고
    • Identification of the Arabidopsis CMS gene as the nitrate reductase structural gene Nia
    • Wilkinson JQ, Crawford NM (1991) Identification of the Arabidopsis CMS gene as the nitrate reductase structural gene Nia. Plant Cell 3: 461-471
    • (1991) Plant Cell , vol.3 , pp. 461-471
    • Wilkinson, J.Q.1    Crawford, N.M.2
  • 48
    • 0027288523 scopus 로고
    • Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes Nia1 and Nia2
    • Wilkinson JQ, Crawford NM (1993) Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes Nia1 and Nia2. Mol Gen Genet 239: 289-297
    • (1993) Mol Gen Genet , vol.239 , pp. 289-297
    • Wilkinson, J.Q.1    Crawford, N.M.2


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