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Volumn 348, Issue 2, 2000, Pages 315-320

Oxalomalate, a competitive inhibitor of aconitase, modulates the RNA-binding activity of iron-regulatory proteins

Author keywords

hydroxy oxalosuccinic acid; Iron metabolism; RNA binding protein

Indexed keywords

ACONITATE HYDRATASE; ENZYME INHIBITOR; GLYOXYLIC ACID; IRON REGULATORY FACTOR; MERCAPTOETHANOL; OXALOACETIC ACID; OXALOMALATE; UNCLASSIFIED DRUG;

EID: 0034212588     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3480315     Document Type: Article
Times cited : (24)

References (28)
  • 1
    • 0013690815 scopus 로고
    • Inhibition of aconitase by glyoxylate plus oxaloacetate
    • 1 Ruffo, A., Romano, M. and Adinolfi, A. (1959) Inhibition of aconitase by glyoxylate plus oxaloacetate. Biochem. J. 72, 613-618
    • (1959) Biochem. J. , vol.72 , pp. 613-618
    • Ruffo, A.1    Romano, M.2    Adinolfi, A.3
  • 2
    • 0013690816 scopus 로고
    • Control of the citric acid cycle by glyoxylate. 1. A new inhibitor of aconitase formed by the condensation of glyoxylate with oxaloacetale
    • 2 Ruffo, A., Testa, E , Adinolfi, A. and Pelizza, G. (1962) Control of the citric acid cycle by glyoxylate. 1. A new inhibitor of aconitase formed by the condensation of glyoxylate with oxaloacetale. Biochem. J. 85, 588-593
    • (1962) Biochem. J. , vol.85 , pp. 588-593
    • Ruffo, A.1    Testa, E.2    Adinolfi, A.3    Pelizza, G.4
  • 3
    • 0013651691 scopus 로고
    • Control of the citric acid cycle by glyoxylate 2 Mechanism of the inhibition of respiration in liver and kidney particles
    • 3 Ruffo, A , Adinolfi, A., Budillon, G. and Capobianco, G. (1962) Control of the citric acid cycle by glyoxylate 2 Mechanism of the inhibition of respiration in liver and kidney particles. Biochem. J. 85, 593-596
    • (1962) Biochem. J. , vol.85 , pp. 593-596
    • Ruffo, A.1    Adinolfi, A.2    Budillon, G.3    Capobianco, G.4
  • 4
    • 0014073086 scopus 로고
    • Control of the citric acid cycle by glyoxylate. Mechanism of the inhibition by oxalomalate and γ-hydroxy-α-oxoglutarate
    • 4 Ruffo, A., Testa, E., Adinolfi, A., Pelizza, G. and Moratti, R. (1967) Control of the citric acid cycle by glyoxylate. Mechanism of the inhibition by oxalomalate and γ-hydroxy-α-oxoglutarate. Biochem. J. 103, 19-23
    • (1967) Biochem. J. , vol.103 , pp. 19-23
    • Ruffo, A.1    Testa, E.2    Adinolfi, A.3    Pelizza, G.4    Moratti, R.5
  • 5
    • 0014575330 scopus 로고
    • Control of the citric acid cycle by glyoxylate. The mechanism of inhibition of oxoglutarate dehydrogenase, isocitrate dehydrogenase and aconitate hydratase
    • 5 Adinolfi, A., Moratti, R., Olezza, S. and Ruffo, A. (1969) Control of the citric acid cycle by glyoxylate. The mechanism of inhibition of oxoglutarate dehydrogenase, isocitrate dehydrogenase and aconitate hydratase. Biochem. J 114, 513-518
    • (1969) Biochem. J , vol.114 , pp. 513-518
    • Adinolfi, A.1    Moratti, R.2    Olezza, S.3    Ruffo, A.4
  • 6
    • 0015155226 scopus 로고
    • Inhibition by oxalomalate of rat liver mitochondrial and extramitochondrial aconitate hydratase
    • 6 Adinolfi, A., Guarriera-Bobyleva, V., Olezza, S. and Ruffo, A. (1971) Inhibition by oxalomalate of rat liver mitochondrial and extramitochondrial aconitate hydratase Biochem. J. 125, 557-562
    • (1971) Biochem. J. , vol.125 , pp. 557-562
    • Adinolfi, A.1    Guarriera-Bobyleva, V.2    Olezza, S.3    Ruffo, A.4
  • 7
    • 0015697612 scopus 로고
    • Citrate metabolism in liver of rats treated with glyoxylate and oxaloacetate
    • 7 Adinolfi, A., Speranza, M. L., Guarriera-Bobyleva, V and Ruffo, A. (1973) Citrate metabolism in liver of rats treated with glyoxylate and oxaloacetate. Ital. J. Biochem. 22, 92-104
    • (1973) Ital. J. Biochem. , vol.22 , pp. 92-104
    • Adinolfi, A.1    Speranza, M.L.2    Guarriera-Bobyleva, V.3    Ruffo, A.4
  • 8
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The conlrol of cellular iron metabolism
    • 8 Klausner, R. D., Rouault, T. A. and Harford, J. B. (1993) Regulating the fate of mRNA: the conlrol of cellular iron metabolism. Cell 72, 19-28
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 9
    • 0027751714 scopus 로고
    • Iron regulatory factor - The conductor of cellular iron regulation
    • 9 Melefors, Ö. and Hentze, M. W. (1993) Iron regulatory factor - the conductor of cellular iron regulation. Blood Rev. 7, 251-258
    • (1993) Blood Rev. , vol.7 , pp. 251-258
    • Melefors, O.1    Hentze, M.W.2
  • 10
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • 10 Hentze, M. W. and Kühn, L. C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci U.S.A 93, 8175-8182
    • (1996) Proc. Natl. Acad. Sci U.S.A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 11
    • 0029930904 scopus 로고    scopus 로고
    • Iron-sulfur clusters as biosensors of oxidants and iron
    • 11 Rouault, T. A. and Klausner, R. D. (1996) Iron-sulfur clusters as biosensors of oxidants and iron. Trends Biochem. Sci. 21, 174-177
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 174-177
    • Rouault, T.A.1    Klausner, R.D.2
  • 12
    • 0032410688 scopus 로고    scopus 로고
    • Iron regulatory proteins, iron responsive elements and iron homeostasis
    • 12 Eisenstein, R. S. and Blemings, K. P. (1998) Iron regulatory proteins, iron responsive elements and iron homeostasis. J. Nutr. 128, 2295-2298
    • (1998) J. Nutr. , vol.128 , pp. 2295-2298
    • Eisenstein, R.S.1    Blemings, K.P.2
  • 13
    • 0031605379 scopus 로고    scopus 로고
    • The iron responsive element (IRE) family of mRNA regulators
    • Sigel, A. and Sigel, H., eds., Marcel Dekker, New York
    • 13 Theil, E. C. (1998) The iron responsive element (IRE) family of mRNA regulators. In Metal lons in Biological Systems, vol. 35 (Sigel, A. and Sigel, H., eds.), pp. 403-434, Marcel Dekker, New York
    • (1998) Metal Lons in Biological Systems , vol.35 , pp. 403-434
    • Theil, E.C.1
  • 15
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron responsive element-binding protein without aconitase activity
    • 15 Guo, B , Yu, Y. and Leibold, E. A. (1994) Iron regulates cytoplasmic levels of a novel iron responsive element-binding protein without aconitase activity J Biol. Chem. 269, 24252-24260
    • (1994) J Biol. Chem. , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 16
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: The bifunctional iron regulatory protein-1
    • 16 Paraskeva, E and Hentze, M W (1996) Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. FEBS Lett. 389, 40-43
    • (1996) FEBS Lett. , vol.389 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 17
    • 0026062191 scopus 로고
    • Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase functional implications
    • 17 Rouault, T. A., Stout, C. D., Kaptain, S., Harford, J. B and Klausner, R D. (1991) Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase functional implications Cell 64, 881-883
    • (1991) Cell , vol.64 , pp. 881-883
    • Rouault, T.A.1    Stout, C.D.2    Kaptain, S.3    Harford, J.B.4    Klausner, R.D.5
  • 18
    • 0027323957 scopus 로고
    • Modification of a free Fe-S cluster cysteine residue in the active iron-responsive element-binding protein prevents RNA binding
    • 18 Philpott, C. C., Haile, D., Rouault, T. A. and Klausner, R. D. (1993) Modification of a free Fe-S cluster cysteine residue in the active iron-responsive element-binding protein prevents RNA binding. J. Biol. Chem. 268, 17655-17658
    • (1993) J. Biol. Chem. , vol.268 , pp. 17655-17658
    • Philpott, C.C.1    Haile, D.2    Rouault, T.A.3    Klausner, R.D.4
  • 19
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • 19 Hirling, H., Henderson, B R. and Kühn, L C. (1994) Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase. EMBO J 13, 453-461
    • (1994) EMBO J , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kühn, L.C.3
  • 20
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • 20 Kennedy, M. C., Emptage, M. H., Dreyer, J L. and Beinert, H. (1983) The role of iron in the activation-inactivation of aconitase. J Biol. Chem. 258, 11098-11105
    • (1983) J Biol. Chem. , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.L.3    Beinert, H.4
  • 21
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulphur cluster results in high-affinity RNA binding
    • 21 Haile, D. J., Rouault, T A., Harford, J. B., Kennedy, M. C., Blondin, G. A., Beinert, H. and Klausner, R. D. (1992) Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulphur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. U.S.A. 89, 11735-11739
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 22
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2)
    • 22 Guo, B., Brown, F. M., Phillips, J. D., Yu, Y. and Leibold, E. A. (1995) Characterization and expression of iron regulatory protein 2 (IRP2). J. Biol. Chem. 270, 16529-16535
    • (1995) J. Biol. Chem. , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 23
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • 23 Iwai, K., Klausner, R. D. and Rouault, T. A. (1995) Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 14, 5350-5357
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 24
    • 0000611266 scopus 로고    scopus 로고
    • Preferential activation of iron regulatory protein-2 in cell lines as a result of higher sensitivity to iron
    • 24 Recalcati, S., Conte, D. and Cairo, G. (1999) Preferential activation of iron regulatory protein-2 in cell lines as a result of higher sensitivity to iron Eur. J. Biochem. 259, 304-309
    • (1999) Eur. J. Biochem. , vol.259 , pp. 304-309
    • Recalcati, S.1    Conte, D.2    Cairo, G.3
  • 25
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction
    • 25 Hentze, M. W., Rouault, T. A., Harford, J. B. and Klausner, R. D. (1989) Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science 244, 357-359
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 26
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • 26 Guo, B., Phillips, J. D., Yu, Y. and Leibold, E. A. (1995) Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem 270, 21645-21651
    • (1995) J. Biol. Chem , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 27
    • 0029132168 scopus 로고
    • Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron
    • 27 Henderson, B. R. and Kühn, L. C. (1995) Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron. J. Biol. Chem. 270, 20509-20515
    • (1995) J. Biol. Chem. , vol.270 , pp. 20509-20515
    • Henderson, B.R.1    Kühn, L.C.2
  • 28
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active-site residues in ligand binding and regulation
    • 28 Philpott, C. C., Klausner, R. D. and Rouault, T. A. (1994) The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc. Natl. Acad. Sci. U.S.A. 91, 7321-7325
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.