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Volumn 128, Issue 1, 2006, Pages 38-47

Glucose-signalled inhibition of cysteine-proteases involved in nitrate reductase degradation in oat leaf segments

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; GLUCOSE; METABOLISM; POLYETHYLENE GLYCOLS;

EID: 33747103047     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2006.00725.x     Document Type: Article
Times cited : (2)

References (53)
  • 1
    • 0000149428 scopus 로고    scopus 로고
    • Induction of a carbon-starvation-related proteolysis in whole maize plants submitted to light/dark cycles and to extended darkness
    • Brouquisse R, Gaudillere J-P, Raymond P (1998) Induction of a carbon-starvation-related proteolysis in whole maize plants submitted to light/dark cycles and to extended darkness. Plant Physiol. 117: 1281-1291
    • (1998) Plant Physiol. , vol.117 , pp. 1281-1291
    • Brouquisse, R.1    Gaudillere, J.-P.2    Raymond, P.3
  • 2
    • 0035103038 scopus 로고    scopus 로고
    • Regulation of protein degradation and protease expression by mannose in maize root tips. Pi sequestration by mannose may hinder the study of its signaling properties
    • Brouquisse R, Evrard A, Rolin D, Raymond P, Roby C (2001) Regulation of protein degradation and protease expression by mannose in maize root tips. Pi sequestration by mannose may hinder the study of its signaling properties. Plant Physiol. 125: 1485-1498
    • (2001) Plant Physiol. , vol.125 , pp. 1485-1498
    • Brouquisse, R.1    Evrard, A.2    Rolin, D.3    Raymond, P.4    Roby, C.5
  • 4
    • 0034660447 scopus 로고    scopus 로고
    • 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells
    • Cotelle V, Meek SEM, Provan F, Milne FC, Morrice N, MacKintosh C (2000) 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells. EMBO J. 19: 2869-2876
    • (2000) EMBO J. , vol.19 , pp. 2869-2876
    • Cotelle, V.1    Meek, S.E.M.2    Provan, F.3    Milne, F.C.4    Morrice, N.5    MacKintosh, C.6
  • 5
    • 0000549163 scopus 로고
    • Tunstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene
    • Deng M, Moureaux T, Caboche M (1989) Tunstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene. Plant Physiol. 91: 304-309
    • (1989) Plant Physiol. , vol.91 , pp. 304-309
    • Deng, M.1    Moureaux, T.2    Caboche, M.3
  • 6
    • 0033729470 scopus 로고    scopus 로고
    • Multiple signaling pathways in gene expression during sugar starvation. Pharmacological analysis of din gene expression in suspension-cultured cells of Arabidopsis
    • Fujiki Y, Ito M, Nishida I, Watanabe A (2000) Multiple signaling pathways in gene expression during sugar starvation. Pharmacological analysis of din gene expression in suspension-cultured cells of Arabidopsis. Plant Physiol. 124: 1139-1147
    • (2000) Plant Physiol. , vol.124 , pp. 1139-1147
    • Fujiki, Y.1    Ito, M.2    Nishida, I.3    Watanabe, A.4
  • 7
    • 0034520162 scopus 로고    scopus 로고
    • Plant sugar-response pathways. Part of a complex regulatory web
    • Gibson SI (2000) Plant sugar-response pathways. Part of a complex regulatory web. Plant Physiol. 124: 1532-1539
    • (2000) Plant Physiol. , vol.124 , pp. 1532-1539
    • Gibson, S.I.1
  • 8
    • 33747125581 scopus 로고    scopus 로고
    • Occurrence of proteins that preferentially inactivate pNR in oat (Avena sativa L.) leaves
    • González C, Kirkwood C, Kenis JD (2000) Occurrence of proteins that preferentially inactivate pNR in oat (Avena sativa L.) leaves. Phyton 69: 109-118
    • (2000) Phyton , vol.69 , pp. 109-118
    • González, C.1    Kirkwood, C.2    Kenis, J.D.3
  • 11
    • 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
  • 12
    • 0038250347 scopus 로고
    • Action of a thiol protease on nitrate reductase in leaves of Hordeum distichum L.
    • Hamano T, Oji Y, Mitsuhashi Y, Matsuki Y, Okamoto S (1984a) Action of a thiol protease on nitrate reductase in leaves of Hordeum distichum L. Plant Cell Physiol. 25: 469-475
    • (1984) Plant Cell Physiol. , vol.25 , pp. 469-475
    • Hamano, T.1    Oji, Y.2    Mitsuhashi, Y.3    Matsuki, Y.4    Okamoto, S.5
  • 13
    • 0038588883 scopus 로고
    • Purification and characterization of thiol protease as a nitrate reductase-inactivating factor from leaves of Hordeum distichum L.
    • Hamano T, Oji Y, Okamoto S, Mitsuhashi Y, Matsuki Y (1984b) Purification and characterization of thiol protease as a nitrate reductase-inactivating factor from leaves of Hordeum distichum L. Plant Cell Physiol. 25: 419-427
    • (1984) Plant Cell Physiol. , vol.25 , pp. 419-427
    • Hamano, T.1    Oji, Y.2    Okamoto, S.3    Mitsuhashi, Y.4    Matsuki, Y.5
  • 14
    • 33747137775 scopus 로고
    • Inverse correlation of Thiol protease with nitrate reductase activities in barley leaves
    • Hamano T, Oji Y, Okamoto S, Mitsuhashi Y, Matsuki Y (1985) Inverse correlation of Thiol protease with nitrate reductase activities in barley leaves. Plant Cell Physiol. 26: 1285-1289
    • (1985) Plant Cell Physiol. , vol.26 , pp. 1285-1289
    • Hamano, T.1    Oji, Y.2    Okamoto, S.3    Mitsuhashi, Y.4    Matsuki, Y.5
  • 15
    • 4544278030 scopus 로고    scopus 로고
    • Nitrate reductase dephosphorylation is induced by sugars and sugar-phosphates in corn leaf segments
    • Iglesias-Bartolome R, González C, Kenis JD (2004) Nitrate reductase dephosphorylation is induced by sugars and sugar-phosphates in corn leaf segments. Physiol. Plant. 122: 62-67
    • (2004) Physiol. Plant. , vol.122 , pp. 62-67
    • Iglesias-Bartolome, R.1    González, C.2    Kenis, J.D.3
  • 16
    • 0029823194 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots
    • James F, Brouquisse R, Suire C, Pradet A, Raymond P (1996) Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots. Biochem. J. 320: 283-292
    • (1996) Biochem. J. , vol.320 , pp. 283-292
    • James, F.1    Brouquisse, R.2    Suire, C.3    Pradet, A.4    Raymond, P.5
  • 17
    • 1842376846 scopus 로고    scopus 로고
    • Hexokinase as a sugars sensor in higher plants
    • Jang J-C, León P, Zhou L, Sheen J (1997) Hexokinase as a sugars sensor in higher plants. Plant Cell 9: 5-19
    • (1997) Plant Cell , vol.9 , pp. 5-19
    • Jang, J.-C.1    León, P.2    Zhou, L.3    Sheen, J.4
  • 18
    • 0034792284 scopus 로고    scopus 로고
    • Post-translational regulation of nitrate reductase: Mechanism, physiological relevance and environmental triggers
    • Kaiser WM, Huber SC (2001) Post-translational regulation of nitrate reductase: mechanism, physiological relevance and environmental triggers. J. Exp. Bot. (Special Issue) 52: 1-9
    • (2001) J. Exp. Bot. (Special Issue) , vol.52 , pp. 1-9
    • Kaiser, W.M.1    Huber, S.C.2
  • 19
    • 0032940292 scopus 로고    scopus 로고
    • Nitrate reductase in higher plants: A case study for transduction of environmental stimuli into control of catalytic activity
    • Kaiser WM, Weiner H, Huber SC (1999) Nitrate reductase in higher plants: a case study for transduction of environmental stimuli into control of catalytic 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
  • 20
    • 0028312453 scopus 로고
    • Inhibition of nitrate reductase by oxygen and water stress in detached oat leaves: A preliminary report on a possible mechanism of action
    • Kenis JD, Rouby MB, Edelman MO, Silvente ST (1994) Inhibition of nitrate reductase by oxygen and water stress in detached oat leaves: A preliminary report on a possible mechanism of action. J. Plant Physiol. 144: 735-739
    • (1994) J. Plant Physiol. , vol.144 , pp. 735-739
    • Kenis, J.D.1    Rouby, M.B.2    Edelman, M.O.3    Silvente, S.T.4
  • 21
    • 14544307565 scopus 로고    scopus 로고
    • Stress-induced changes in protease composition are determined by nitrogen supply in non-nodulating whiteclover
    • Kingston-Smith AH, Bollard AL, Minchin FR (2005) Stress-induced changes in protease composition are determined by nitrogen supply in non-nodulating whiteclover. J. Exp. Bot. 56: 745-753
    • (2005) J. Exp. Bot. , vol.56 , pp. 745-753
    • Kingston-Smith, A.H.1    Bollard, A.L.2    Minchin, F.R.3
  • 22
    • 0031279985 scopus 로고    scopus 로고
    • Calcium signalling in Arabidopsis thaliana responding to drought and salinity
    • Knight H, Trewavas AJ, Knight MR (1997) Calcium signalling in Arabidopsis thaliana responding to drought and salinity. Plant J. 12: 1067-1078
    • (1997) Plant J. , vol.12 , pp. 1067-1078
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 25
    • 2942567827 scopus 로고    scopus 로고
    • Mechanism and importance of post-translational regulation of nitrate reductase
    • Lillo C, Meyer C, Lea US, Provan F, Oltedal S (2004) Mechanism and importance of post-translational regulation of nitrate reductase. J. Exp. Bot. 55: 1275-1282
    • (2004) J. Exp. Bot. , vol.55 , pp. 1275-1282
    • Lillo, C.1    Meyer, C.2    Lea, U.S.3    Provan, F.4    Oltedal, S.5
  • 26
    • 0033939985 scopus 로고    scopus 로고
    • Glucose and disaccharide-sensing mechanisms modulate the expression of α-amylase in barley embryos
    • Loreti E, Alpi A, Perata P (2000) Glucose and disaccharide-sensing mechanisms modulate the expression of α-amylase in barley embryos. Plant Physiol. 123: 939-948
    • (2000) Plant Physiol. , vol.123 , pp. 939-948
    • Loreti, E.1    Alpi, A.2    Perata, P.3
  • 27
    • 0035103179 scopus 로고    scopus 로고
    • Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis
    • MacKintosh C, Meek SEM (2001) Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis. Cell. Mol. Life Sci. 58: 205-214
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 205-214
    • MacKintosh, C.1    Meek, S.E.M.2
  • 28
    • 0028795834 scopus 로고
    • Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro
    • McMichael RW, Jr, Bachmann M, Huber SC (1995) Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro. Plant Physiol 108: 1077-1082
    • (1995) Plant Physiol. , vol.108 , pp. 1077-1082
    • McMichael Jr., R.W.1    Bachmann, M.2    Huber, S.C.3
  • 29
    • 0035873250 scopus 로고    scopus 로고
    • Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal
    • Moriya H, Shimizu-Yoshida Y, Omori A, Iwashita S, Katoh M, Sakai A (2001) Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal. Genes Dev. 15: 1217-1228
    • (2001) Genes Dev. , vol.15 , pp. 1217-1228
    • Moriya, H.1    Shimizu-Yoshida, Y.2    Omori, A.3    Iwashita, S.4    Katoh, M.5    Sakai, A.6
  • 30
    • 85047686009 scopus 로고    scopus 로고
    • Different sugar kinases are involved in the sugar sensing of Galdieria sulphuraria
    • Oesterhelt C, Gross W (2002) Different sugar kinases are involved in the sugar sensing of Galdieria sulphuraria. Plant Physiol. 128: 291-299.
    • (2002) Plant Physiol. , vol.128 , pp. 291-299
    • Oesterhelt, C.1    Gross, W.2
  • 31
    • 0029187864 scopus 로고
    • Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco
    • Ohto M, Nakamura K (1995) Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco. Plant Physiol. 109: 973-981
    • (1995) Plant Physiol. , vol.109 , pp. 973-981
    • Ohto, M.1    Nakamura, K.2
  • 32
    • 0029136757 scopus 로고
    • 2+ signalling in the sugar-inducible expression of genes coding for sporamin and α-amylase of sweet potato
    • 2+ signalling in the sugar-inducible expression of genes coding for sporamin and α-amylase of sweet potato. Plant J. 7: 297-307
    • (1995) Plant J. , vol.7 , pp. 297-307
    • Ohto, M.1    Hayashi, K.2    Isobe, M.3    Nakamura, K.4
  • 33
    • 0000098472 scopus 로고
    • Regulation of corn leaf NR. II Synthesis and turnover of the enzyme's activity and protein
    • Remmler JL and Campbell WH (1986) Regulation of corn leaf NR. II Synthesis and turnover of the enzyme's activity and protein. Plant Physiol. 80: 442-447
    • (1986) Plant Physiol. , vol.80 , pp. 442-447
    • Remmler, J.L.1    Campbell, W.H.2
  • 36
    • 0029187144 scopus 로고
    • Regulation of nitrate reductase by nitrate during light-dark transition in detached oat leaves
    • Rouby M, Ponce-Villacís F, Córdoba A, Kenis JD (1995) Regulation of nitrate reductase by nitrate during light-dark transition in detached oat leaves. Plant Cell Physiol. 36: 1399-1403
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1399-1403
    • Rouby, M.1    Ponce-Villacís, F.2    Córdoba, A.3    Kenis, J.D.4
  • 37
    • 2642631759 scopus 로고    scopus 로고
    • Substrates regulate the phosphorylation status of nitrate reductase
    • Rouby M, González CA, Kenis JD (1998) Substrates regulate the phosphorylation status of nitrate reductase. Physiol. Plant. 102: 547-552
    • (1998) Physiol. Plant. , vol.102 , pp. 547-552
    • Rouby, M.1    González, C.A.2    Kenis, J.D.3
  • 38
    • 0001741314 scopus 로고
    • Nitrate reductase activity in maize (Zea mays L.) leaves. I Regulation by nitrate flux
    • Shaner DL, Boyer JS (1976) Nitrate reductase activity in maize (Zea mays L.) leaves. I Regulation by nitrate flux. Plant Physiol. 58: 499-504
    • (1976) Plant Physiol. , vol.58 , pp. 499-504
    • Shaner, D.L.1    Boyer, J.S.2
  • 40
    • 0038250348 scopus 로고
    • In vitro stability of nitrate reductase from wheat leaves. III. Isolation and partial characterization of a nitrate reductase-inactivating factor
    • Sherrard JH, Kennedy JA, Dalling MJ (1979) In vitro stability of nitrate reductase from wheat leaves. III. Isolation and partial characterization of a nitrate reductase-inactivating factor. Plant Physiol. 64: 640-645
    • (1979) Plant Physiol. , vol.64 , pp. 640-645
    • Sherrard, J.H.1    Kennedy, J.A.2    Dalling, M.J.3
  • 41
    • 0031403530 scopus 로고    scopus 로고
    • Sugar sensing and sugar-mediated signal transduction in plants
    • Smeekens S, Rook F (1997) Sugar sensing and sugar-mediated signal transduction in plants. Plant Physiol. 115: 7-13
    • (1997) Plant Physiol. , vol.115 , pp. 7-13
    • Smeekens, S.1    Rook, F.2
  • 44
    • 0033134243 scopus 로고    scopus 로고
    • 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
    • Sugden C, Donaghy PG, Halford NG, Hardie DG (1999) 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. Plant Physiol. 120: 257-274,
    • (1999) Plant Physiol. , vol.120 , pp. 257-274
    • Sugden, C.1    Donaghy, P.G.2    Halford, N.G.3    Hardie, D.G.4
  • 45
    • 0028047087 scopus 로고
    • Inhibitors of protein phosphatases 1 and 2A block the sugar-inducible gene expression in plants
    • Takeda S, Mano S, Ohto M, Nakamura K (1994) Inhibitors of protein phosphatases 1 and 2A block the sugar-inducible gene expression in plants. Plant Physiol. 106: 567-574
    • (1994) Plant Physiol. , vol.106 , pp. 567-574
    • Takeda, S.1    Mano, S.2    Ohto, M.3    Nakamura, K.4
  • 46
    • 0034073253 scopus 로고    scopus 로고
    • Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
    • Toroser D, Plaut Z, Huber SC (2000) Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate. Plant Physiol. 123: 403-411.
    • (2000) Plant Physiol. , vol.123 , pp. 403-411
    • Toroser, D.1    Plaut, Z.2    Huber, S.C.3
  • 47
    • 33747134533 scopus 로고
    • Evidence for an inactivating system of nitrate reductase in Hordeum vulgare L. during darkness that requires protein synthesis
    • Travis RL, Jordan WR, Huffaker RC (1969) Evidence for an inactivating system of nitrate reductase in Hordeum vulgare L. during darkness that requires protein synthesis. Plant Physiol. 44:1150-1156
    • (1969) Plant Physiol. , vol.44 , pp. 1150-1156
    • Travis, R.L.1    Jordan, W.R.2    Huffaker, R.C.3
  • 49
    • 0032999455 scopus 로고    scopus 로고
    • 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves
    • Weiner H, Kaiser WM (1999) 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves. FEBS Lett. 455:75-78
    • (1999) FEBS Lett. , vol.455 , pp. 75-78
    • Weiner, H.1    Kaiser, W.M.2
  • 50
    • 0345073595 scopus 로고
    • Purification and properties of a NR inactivating factor from rice cells in suspension culture
    • Yamaya T, Ohira K (1977) Purification and properties of a NR inactivating factor from rice cells in suspension culture. Plant Cell Physiol. 18:915-925
    • (1977) Plant Cell Physiol. , vol.18 , pp. 915-925
    • Yamaya, T.1    Ohira, K.2
  • 51
    • 0038588893 scopus 로고
    • Characteristics of NR-inactivating proteins obtained from corn roots and rice cell cultures
    • Yamaya T, Oaks A, Boesel IL (1980) Characteristics of NR-inactivating proteins obtained from corn roots and rice cell cultures. Plant Physiol. 65:141-145
    • (1980) Plant Physiol. , vol.65 , pp. 141-145
    • Yamaya, T.1    Oaks, A.2    Boesel, I.L.3
  • 52
    • 0033230737 scopus 로고    scopus 로고
    • Cellular and genetic responses of plants to sugar starvation
    • Yu S-M (1999) Cellular and genetic responses of plants to sugar starvation. Plant Physiol. 121:687-693.
    • (1999) Plant Physiol. , vol.121 , pp. 687-693
    • Yu, S.-M.1
  • 53
    • 0025718505 scopus 로고
    • Metabolic derepression of α-amylase gene expression in suspension-cultured cells of rice
    • Yu S-M, Kuo Y-H, Sheu G, Sheu Y-J, Fei L (1991) Metabolic derepression of α-amylase gene expression in suspension-cultured cells of rice. J. Biol. Chem. 266: 21131-21137
    • (1991) J. Biol. Chem. , vol.266 , pp. 21131-21137
    • Yu, S.-M.1    Kuo, Y.-H.2    Sheu, G.3    Sheu, Y.-J.4    Fei, L.5


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