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Volumn 120, Issue 1, 1999, Pages 257-274

Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme a reductase, nitrate reductase, and sucrose phosphate synthase in vitro

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; AMINO ACID SEQUENCE; ARABIDOPSIS; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; ISOPRENOID; NITRATE REDUCTASE; NITROGEN METABOLISM; PHOSPHORYLATION; PROTEIN KINASE; SUCROSE; SUCROSE PHOSPHATE SYNTHASE;

EID: 0033134243     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.120.1.257     Document Type: Article
Times cited : (242)

References (54)
  • 2
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein
    • Bachmann M, Huber JL, Liao PC, Gage DA, Huber SC (1996a) The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves 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
  • 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 BC, Harmon AC, Huber SC (1996b) 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
    • 0029583202 scopus 로고
    • Immunological evidence that HMG-CoA reductase kinase-A is the cauliflower homologue of the RKIN1 subfamily of plant protein kinases
    • Ball KL, Barker J, Halford NG, Hardie DG (1995) Immunological evidence that HMG-CoA reductase kinase-A is the cauliflower homologue of the RKIN1 subfamily of plant protein kinases. FEBS Lett 377: 189-192
    • (1995) FEBS Lett , vol.377 , pp. 189-192
    • Ball, K.L.1    Barker, J.2    Halford, N.G.3    Hardie, D.G.4
  • 5
    • 0027954963 scopus 로고
    • Biochemical characterization of two forms of 3-hydroxy 3-methylglutaryl CoA reductase kinase from cauliflower (Brassica oleracia)
    • Ball KL, Dale S, Weekes J, Hardie DG (1994) Biochemical characterization of two forms of 3-hydroxy 3-methylglutaryl CoA reductase kinase from cauliflower (Brassica oleracia). Eur J Biochem 219: 743-750
    • (1994) Eur J Biochem , vol.219 , pp. 743-750
    • Ball, K.L.1    Dale, S.2    Weekes, J.3    Hardie, D.G.4
  • 6
    • 0030296153 scopus 로고    scopus 로고
    • Evidence that barley HMG-CoA reductase kinase is a member of the SNF1-related protein kinase family
    • Barker JHA, Slocombe SP, Ball KL, Hardie DG, Shewry PR, Halford NG (1996) Evidence that barley HMG-CoA reductase kinase is a member of the SNF1-related protein kinase family. Plant Physiol 112: 1141-1149
    • (1996) Plant Physiol , vol.112 , pp. 1141-1149
    • Barker, J.H.A.1    Slocombe, S.P.2    Ball, K.L.3    Hardie, D.G.4    Shewry, P.R.5    Halford, N.G.6
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 9
    • 0028310837 scopus 로고
    • Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism
    • Carling D, Aguan K, Woods A, Verhoeven AJM, Beri RK, Brennan CH, Sidebottom C, Davison MD, Scott J (1994) Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. J Biol Chem 269: 11442-11448
    • (1994) J Biol Chem , vol.269 , pp. 11442-11448
    • Carling, D.1    Aguan, K.2    Woods, A.3    Verhoeven, A.J.M.4    Beri, R.K.5    Brennan, C.H.6    Sidebottom, C.7    Davison, M.D.8    Scott, J.9
  • 10
    • 0022534202 scopus 로고
    • A yeast gene that is essential for release from glucose repression encodes a protein kinase
    • Celenza JL, Carlson M (1986) A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science 233: 1175-1180
    • (1986) Science , vol.233 , pp. 1175-1180
    • Celenza, J.L.1    Carlson, M.2
  • 12
    • 85047689953 scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribonucleoside: A specific method for activating AMP-activated protein kinase in intact cells?
    • Corton JM, Gillespie JG, Hawley SA, Hardie DG (1995) 5-Aminoimidazole-4-carboxamide ribonucleoside: a specific method for activating AMP-activated protein kinase in intact cells? Eur J Biochem 229: 558-565
    • (1995) Eur J Biochem , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 13
    • 0028834801 scopus 로고
    • Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase (isoform HMGR1) from Arabidopsis, and its inactivation by phosphorylation at serine-577 by Brassica oleracea 3-hydroxy-3-methylglutaryl CoA reductase kinase
    • Dale S, Arró M, Becerra B, Morrice NG, Boronat A, Hardie DG, Ferrer A (1995a) Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase (isoform HMGR1) from Arabidopsis, and its inactivation by phosphorylation at serine-577 by Brassica oleracea 3-hydroxy-3-methylglutaryl CoA reductase kinase. Eur J Biochem 233: 506-513
    • (1995) Eur J Biochem , vol.233 , pp. 506-513
    • Dale, S.1    Arró, M.2    Becerra, B.3    Morrice, N.G.4    Boronat, A.5    Hardie, D.G.6    Ferrer, A.7
  • 14
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale S, Wilson WA, Edelman AM, Hardie DG (1995b) Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett 361: 191-195
    • (1995) FEBS Lett , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 15
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • Davies SP, Carling D, Hardie DG (1989) Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. Eur J Biochem 186: 123-128
    • (1989) Eur J Biochem , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 16
    • 0028068882 scopus 로고
    • Purification of the AMP-activated protein kinase on ATP-y-Sepharose and analysis of its subunit structure
    • Davies SP, Hawley SA, Woods A, Carling D, Haystead TAJ, Hardie DG (1994) Purification of the AMP-activated protein kinase on ATP-y-Sepharose and analysis of its subunit structure. Eur J Biochem 223: 351-357
    • (1994) Eur J Biochem , vol.223 , pp. 351-357
    • Davies, S.P.1    Hawley, S.A.2    Woods, A.3    Carling, D.4    Haystead, T.A.J.5    Hardie, D.G.6
  • 18
    • 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
  • 21
    • 0031810672 scopus 로고    scopus 로고
    • Yeast carbon catabolite repression
    • Gancedo JM (1998) Yeast carbon catabolite repression. Microbiol Mol Biol Rev 62: 334-361
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 334-361
    • Gancedo, J.M.1
  • 22
    • 0032127148 scopus 로고    scopus 로고
    • SNF1-related protein kinases: Global regulators of carbon metabolism in plants?
    • Halford NG, Hardie DG (1998) SNF1-related protein kinases: global regulators of carbon metabolism in plants? Plant Mol Biol 37: 735-748
    • (1998) Plant Mol Biol , vol.37 , pp. 735-748
    • Halford, N.G.1    Hardie, D.G.2
  • 25
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase: Fuel gauge of the mammalian cell?
    • Hardie DG, Carting D (1997) The AMP-activated protein kinase: fuel gauge of the mammalian cell? Eur J Biochem 246: 259-273
    • (1997) Eur J Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 26
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie DG, Carling D, Carlson M (1998) The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu Rev Biochem 67: 821-855
    • (1998) Annu Rev Biochem , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 27
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase
    • Hawley SA, Davison M, Woods A, Davies SP, Beri RK, Carling D, Hardie DG (1996) Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase. J Biol Chem 271: 27879-27887
    • (1996) J Biol Chem , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 29
    • 0027221568 scopus 로고
    • Gamma-phosphate-linked ATP-Sepharose for the affinity purification of protein kinases: Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase
    • Haystead CMM, Gregory P, Sturgill TW, Haystead TAJ (1993) Gamma-phosphate-linked ATP-Sepharose for the affinity purification of protein kinases: rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase. Eur J Biochem 214: 459-467
    • (1993) Eur J Biochem , vol.214 , pp. 459-467
    • Haystead, C.M.M.1    Gregory, P.2    Sturgill, T.W.3    Haystead, T.A.J.4
  • 30
    • 0024671488 scopus 로고
    • Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose phosphate synthase activity
    • Huber JLA, Huber SC, Nielsen TH (1989) Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose phosphate synthase activity. Arch Biochem Biophys 270: 681-690
    • (1989) Arch Biochem Biophys , vol.270 , pp. 681-690
    • Huber, J.L.A.1    Huber, S.C.2    Nielsen, T.H.3
  • 31
    • 0025131801 scopus 로고
    • Activation of sucrose-phosphate synthase from darkened spinach leaves by an endogenous protein phosphatase
    • Huber SC, Huber JL (1990) Activation of sucrose-phosphate synthase from darkened spinach leaves by an endogenous protein phosphatase. Arch Biochem Biophys 282: 421-426
    • (1990) Arch Biochem Biophys , vol.282 , pp. 421-426
    • Huber, S.C.1    Huber, J.L.2
  • 32
    • 0026090386 scopus 로고
    • In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase
    • Huber SC, Huber JL (1991) In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase. Biochim Biophys Acta 1091: 393-400
    • (1991) Biochim Biophys Acta , vol.1091 , pp. 393-400
    • Huber, S.C.1    Huber, J.L.2
  • 33
    • 0040419081 scopus 로고    scopus 로고
    • Role and regulation of sucrose phosphate synthase in higher plants
    • Huber SC, Huber JL (1996) Role and regulation of sucrose phosphate synthase in higher plants. Annu Rev Plant Physiol Plant Mol Biol 47: 431-444
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 431-444
    • Huber, S.C.1    Huber, J.L.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 35
    • 0026761190 scopus 로고
    • Structure and expression of a gene from Arabidopsis encoding a protein related to SNFl protein kinase
    • Le Guen L, Thomas M, Bianchi M, Halford NG, Kreis M (1992) Structure and expression of a gene from Arabidopsis encoding a protein related to SNFl protein kinase. Gene 120: 249-254
    • (1992) Gene , vol.120 , pp. 249-254
    • Le Guen, L.1    Thomas, M.2    Bianchi, M.3    Halford, N.G.4    Kreis, M.5
  • 36
    • 0029110548 scopus 로고
    • Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves
    • Mackintosh C, Douglas P, Lillo C (1995) Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves. Plant Physiol 107: 451-457
    • (1995) Plant Physiol , vol.107 , pp. 451-457
    • Mackintosh, C.1    Douglas, P.2    Lillo, C.3
  • 38
    • 0031149601 scopus 로고    scopus 로고
    • Potato SNF1-related protein kinase: Molecular cloning, expression analysis and peptide kinase activity measurements
    • Man AL, Purcell PC, Hannappel U, Halford NG (1997) Potato SNF1-related protein kinase: molecular cloning, expression analysis and peptide kinase activity measurements. Plant Mol Biol 34: 31-43
    • (1997) Plant Mol Biol , vol.34 , pp. 31-43
    • Man, A.L.1    Purcell, P.C.2    Hannappel, U.3    Halford, N.G.4
  • 40
    • 0028795834 scopus 로고
    • Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated by multiple protein kinases in vitro
    • McMichael RW, Bachmann M, Huber SC (1995a) Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated by multiple protein kinases in vitro. Plant Physiol 108: 1077-1082
    • (1995) Plant Physiol , vol.108 , pp. 1077-1082
    • McMichael, R.W.1    Bachmann, M.2    Huber, S.C.3
  • 41
    • 0027133515 scopus 로고
    • Identification of the major regulatory phosphorylation site in sucrose phosphate synthase
    • McMichael RW Jr, Klein RR, Salvucci ME, Huber SC (1993) Identification of the major regulatory phosphorylation site in sucrose phosphate synthase. Arch Biochem Biophys 307: 248-252
    • (1993) Arch Biochem Biophys , vol.307 , pp. 248-252
    • McMichael R.W., Jr.1    Klein, R.R.2    Salvucci, M.E.3    Huber, S.C.4
  • 42
    • 0029081381 scopus 로고
    • Characterization of the substrate specificity of sucrose phosphate synthase protein kinase
    • McMichael RW Jr, Kochansky J, Klein RR, Huber SC (1995b) Characterization of the substrate specificity of sucrose phosphate synthase protein kinase. Arch Biochem Biophys 321: 71-75
    • (1995) Arch Biochem Biophys , vol.321 , pp. 71-75
    • McMichael R.W., Jr.1    Kochansky, J.2    Klein, R.R.3    Huber, S.C.4
  • 43
    • 0027932717 scopus 로고
    • Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase
    • Mitchelhill KI, Stapleton D, Gao G, House C, Michell B, Katsis F, Witters LA, Kemp BE (1994) Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J Biol Chem 269: 2361-2364
    • (1994) J Biol Chem , vol.269 , pp. 2361-2364
    • Mitchelhill, K.I.1    Stapleton, D.2    Gao, G.3    House, C.4    Michell, B.5    Katsis, F.6    Witters, L.A.7    Kemp, B.E.8
  • 44
    • 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, Scarabel 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    Scarabel, M.4    Aitken, A.5    MacKintosh, C.6
  • 45
    • 0028274294 scopus 로고
    • Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae
    • Muranaka T, Banno H, Machida Y (1994) Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae. Mol Cell Biol 14: 2958-2965
    • (1994) Mol Cell Biol , vol.14 , pp. 2958-2965
    • Muranaka, T.1    Banno, H.2    Machida, Y.3
  • 46
    • 0031861675 scopus 로고    scopus 로고
    • Antisense expression of a sucrose non-fermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibiliry of sucrose synthase transcripts in leaves
    • Purcell PC, Smith AM, Halford NG (1998) Antisense expression of a sucrose non-fermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibiliry of sucrose synthase transcripts in leaves. Plant J 14: 195-202
    • (1998) Plant J , vol.14 , pp. 195-202
    • Purcell, P.C.1    Smith, A.M.2    Halford, N.G.3
  • 47
    • 0002437089 scopus 로고
    • Partial purification of 2 forms of spinach leaf sucrose phosphate synthase which differ in their kinetic properties
    • Siegl G, Stitt M (1990) Partial purification of 2 forms of spinach leaf sucrose phosphate synthase which differ in their kinetic properties. Plant Sci 66: 205-210
    • (1990) Plant Sci , vol.66 , pp. 205-210
    • Siegl, G.1    Stitt, M.2
  • 49
    • 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
  • 51
    • 0027440990 scopus 로고
    • Specificity determinants for the AMP-activated protein kinase and its plant homologue analyzed using synthetic peptides
    • Weekes J, Ball KL, Caudwell FB, Hardie DG (1993) Specificity determinants for the AMP-activated protein kinase and its plant homologue analyzed using synthetic peptides. FEBS Lett 334: 335-339
    • (1993) FEBS Lett , vol.334 , pp. 335-339
    • Weekes, J.1    Ball, K.L.2    Caudwell, F.B.3    Hardie, D.G.4
  • 52
    • 0028812010 scopus 로고
    • Antibodies that distinguish between the serine-158 phospho-form and dephospho-form of spinach leaf sucrose-phosphate synthase
    • Weiner H (1995) Antibodies that distinguish between the serine-158 phospho-form and dephospho-form of spinach leaf sucrose-phosphate synthase. Plant Physiol 108: 219-225
    • (1995) Plant Physiol , vol.108 , pp. 219-225
    • Weiner, H.1
  • 53
    • 0030293885 scopus 로고    scopus 로고
    • The mechanism of glucose repression/derepression in yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio
    • Wilson WA, Hawley SA Hardie DG (1996) The mechanism of glucose repression/derepression in yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio. Curr Biol 6: 1426-1434
    • (1996) Curr Biol , vol.6 , pp. 1426-1434
    • Wilson, W.A.1    Hawley, S.A.2    Hardie, D.G.3
  • 54
    • 0030592623 scopus 로고    scopus 로고
    • The aα1 and α2. isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • Woods A, Salt I, Scott J, Hardie DG, Carling D (1996) The aα1 and α2. isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Lett 397: 347-351
    • (1996) FEBS Lett , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5


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