메뉴 건너뛰기




Volumn 7, Issue 1, 2014, Pages 156-169

Redox regulation of arabidopsis mitochondrial citrate synthase

Author keywords

Arabidopsis; Citrate synthase; Cysteine residues; Mitochondria; Redox regulation; TCA cycle; Thioredoxin

Indexed keywords

CITRATE SYNTHASE; CYSTEINE; DISULFIDE; HYDROGEN PEROXIDE; ISOENZYME; THIOREDOXIN;

EID: 84891796908     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/sst144     Document Type: Article
Times cited : (83)

References (52)
  • 1
    • 0042009669 scopus 로고    scopus 로고
    • Modulation of citrate metabolism alters aluminum tolerance in yeast and transgenic canola overexpressing a mitochondrial citrate synthase
    • Anoop, V.M., Basu, U., McCammon, M.T., McAlister-Henn, L., and Taylor, G.J. (2003). Modulation of citrate metabolism alters aluminum tolerance in yeast and transgenic canola overexpressing a mitochondrial citrate synthase. Plant Physiol. 132, 2205-2217.
    • (2003) Plant Physiol. , vol.132 , pp. 2205-2217
    • Anoop, V.M.1    Basu, U.2    McCammon, M.T.3    McAlister-Henn, L.4    Taylor, G.J.5
  • 2
    • 83255187370 scopus 로고    scopus 로고
    • Metabolic control and regulation of the tricarboxylic acid cycle in photosynthetic and heterotrophic plant tissues
    • Araujo, W.L., Nunes-Nesi, A., Nikoloski, Z., Sweetlove, L.J., and Fernie, A.R. (2012). Metabolic control and regulation of the tricarboxylic acid cycle in photosynthetic and heterotrophic plant tissues. Plant Cell Environ. 35, 1-21.
    • (2012) Plant Cell Environ. , vol.35 , pp. 1-21
    • Araujo, W.L.1    Nunes-Nesi, A.2    Nikoloski, Z.3    Sweetlove, L.J.4    Fernie, A.R.5
  • 4
    • 51749120178 scopus 로고    scopus 로고
    • Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o
    • Barranco-Medina, S., Krell, T., Bernier-Villamor, L., Sevilla, F., Lazaro, J.J., and Dietz, K.J. (2008). Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o. J. Exp. Bot. 59, 3259-3269.
    • (2008) J. Exp. Bot. , vol.59 , pp. 3259-3269
    • Barranco-Medina, S.1    Krell, T.2    Bernier-Villamor, L.3    Sevilla, F.4    Lazaro, J.J.5    Dietz, K.J.6
  • 5
    • 0021452388 scopus 로고
    • The ferredoxin/thioredoxin system: A key element in the regulatory function of light in photosynthesis
    • Buchanan, B.B. (1984). The ferredoxin/thioredoxin system: a key element in the regulatory function of light in photosynthesis. Bioscience. 34, 378-383.
    • (1984) Bioscience. , vol.34 , pp. 378-383
    • Buchanan, B.B.1
  • 6
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized P.P.B.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008). MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotech. 26, 1367-1372.
    • (2008) Nat. Biotech. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 8
    • 67649518065 scopus 로고    scopus 로고
    • Overexpression of Citrus junos mitochondrial citrate synthase gene in Nicotiana benthamiana confers aluminum tolerance
    • Deng, W., Luo, K., Li, Z., Yang, Y., Hu, N., and Wu, Y. (2009). Overexpression of Citrus junos mitochondrial citrate synthase gene in Nicotiana benthamiana confers aluminum tolerance. Planta. 230, 355-365.
    • (2009) Planta. , vol.230 , pp. 355-365
    • Deng, W.1    Luo, K.2    Li, Z.3    Yang, Y.4    Hu, N.5    Wu, Y.6
  • 9
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and von Heijne, G. (2000). Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300, 1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 10
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • Finkemeier, I., Goodman, M., Lamkemeyer, P., Kandlbinder, A., Sweetlove, L.J., and Dietz, K.J. (2005). The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280, 12168-12180.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12168-12180
    • Finkemeier, I.1    Goodman, M.2    Lamkemeyer, P.3    Kandlbinder, A.4    Sweetlove, L.J.5    Dietz, K.J.6
  • 13
    • 70349327670 scopus 로고    scopus 로고
    • One novel mitochondrial citrate synthase from Oryza sativa L. Can Enhance Aluminum Tolerance in Transgenic Tobacco
    • Han, Y., Zhang, W., Zhang, B., Zhang, S., Wang, W., and Ming, F. (2009). One novel mitochondrial citrate synthase from Oryza sativa L. can enhance aluminum tolerance in transgenic tobacco. Mol. Biotech. 42, 299-305.
    • (2009) Mol. Biotech. , vol.42 , pp. 299-305
    • Han, Y.1    Zhang, W.2    Zhang, B.3    Zhang, S.4    Wang, W.5    Ming, F.6
  • 14
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood, J.L., Tonti-Filippini, J.S., Gout, A.M., Day, D.A., Whelan, J., and Millar, A.H. (2004). Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell. 16, 241-256.
    • (2004) Plant Cell. , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 15
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • Horling, F., Lamkemeyer, P., Konig, J., Finkemeier, I., Kandlbinder, A., Baier, M., and Dietz, K.J. (2003). Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol. 131, 317-325.
    • (2003) Plant Physiol. , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    Konig, J.3    Finkemeier, I.4    Kandlbinder, A.5    Baier, M.6    Dietz, K.J.7
  • 16
    • 33947537310 scopus 로고
    • Properties of citrate synthase from Pisum sativum mitochondria
    • Iredale, S.E. (1979). Properties of citrate synthase from Pisum sativum mitochondria. Phytochemistry. 18, 1057-1057.
    • (1979) Phytochemistry. , vol.18 , pp. 1057-1057
    • Iredale, S.E.1
  • 17
    • 38249031190 scopus 로고
    • Citrate synthase and malate dehydrogenase from tomato fruit
    • Jeffery, D., Goodenough, P.W., and Weitzman, P.D.J. (1988). Citrate synthase and malate dehydrogenase from tomato fruit. Phytochemistry. 27, 41-44.
    • (1988) Phytochemistry. , vol.27 , pp. 41-44
    • Jeffery, D.1    Goodenough, P.W.2    Weitzman, P.D.J.3
  • 18
    • 0017775681 scopus 로고
    • Substrate-inhibition by acetyl-CoA in condensation reaction between oxaloacetate and acetyl-CoA catalyzed by citrate synthase from pig heart
    • Johansson, C.J., and Pettersson, G. (1977). Substrate-inhibition by acetyl-CoA in condensation reaction between oxaloacetate and acetyl-CoA catalyzed by citrate synthase from pig heart. Biochim. Biophys. Acta. 484, 208-215.
    • (1977) Biochim. Biophys. Acta. , vol.484 , pp. 208-215
    • Johansson, C.J.1    Pettersson, G.2
  • 19
    • 76649119460 scopus 로고    scopus 로고
    • Nonlinear least-squares data fitting in Excel spreadsheets
    • Kemmer, G., and Keller, S. (2010). Nonlinear least-squares data fitting in Excel spreadsheets. Nat. Protoc. 5, 267-281.
    • (2010) Nat. Protoc. , vol.5 , pp. 267-281
    • Kemmer, G.1    Keller, S.2
  • 20
    • 80053594838 scopus 로고    scopus 로고
    • Defining the protein complex proteome of plant mitochondria
    • Klodmann, J., Senkler, M., Rode, C., and Braun, H.P. (2011). Defining the protein complex proteome of plant mitochondria. Plant Physiol. 157, 587-598.
    • (2011) Plant Physiol. , vol.157 , pp. 587-598
    • Klodmann, J.1    Senkler, M.2    Rode, C.3    Braun, H.P.4
  • 21
    • 84861706924 scopus 로고    scopus 로고
    • Mechanisms and dynamics in the thiol/disulfide redox regulatory network: Transmitters, sensors and targets
    • König, J., Muthuramalingam, M., and Dietz, K.J. (2012). Mechanisms and dynamics in the thiol/disulfide redox regulatory network: transmitters, sensors and targets. Curr. Opin. Plant Biol. 15, 261-268.
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 261-268
    • König, J.1    Muthuramalingam, M.2    Dietz, K.J.3
  • 22
    • 0028799231 scopus 로고
    • Catalytic strategy of citrate synthase-subunit interactions revealed as a consequence of a single amino-acid change in the oxaloacetate binding-site
    • Kurz, L.C., Shah, S., Frieden, C., Nakra, T., Stein, R.E., Drysdale, G.R., Evans, C.T., and Srere, P.A. (1995). Catalytic strategy of citrate synthase-subunit interactions revealed as a consequence of a single amino-acid change in the oxaloacetate binding-site. Biochemistry. 34, 13278-13288.
    • (1995) Biochemistry. , vol.34 , pp. 13278-13288
    • Kurz, L.C.1    Shah, S.2    Frieden, C.3    Nakra, T.4    Stein, R.E.5    Drysdale, G.R.6    Evans, C.T.7    Srere, P.A.8
  • 25
    • 1842434524 scopus 로고    scopus 로고
    • The role of phosphorus in aluminium-induced citrate and malate exudation from rape (Brassica napus)
    • Ligaba, A., Shen, H., Shibata, K., Yamamoto, Y., Tanakamaru, S., and Matsumoto, H. (2004). The role of phosphorus in aluminium-induced citrate and malate exudation from rape (Brassica napus). Physiol. Plant. 120, 575-584.
    • (2004) Physiol. Plant. , vol.120 , pp. 575-584
    • Ligaba, A.1    Shen, H.2    Shibata, K.3    Yamamoto, Y.4    Tanakamaru, S.5    Matsumoto, H.6
  • 27
    • 84865411350 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin systems in plants: Molecular mechanisms, crosstalks, and functional significance
    • Meyer, Y., Belin, C., Delorme-Hinoux, V., Reichheld, J.P., and Riondet, C. (2012). Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance. Antioxidants & Redox Signaling. 17, 1124-1160.
    • (2012) Antioxidants & Redox Signaling. , vol.17 , pp. 1124-1160
    • Meyer, Y.1    Belin, C.2    Delorme-Hinoux, V.3    Reichheld, J.P.4    Riondet, C.5
  • 28
    • 67649880593 scopus 로고    scopus 로고
    • NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts
    • Michalska, J., Zauber, H., Buchanan, B.B., Cejudo, F.J., and Geigenberger, P. (2009). NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts. Proc. Natl Acad. Sci. U S A. 106, 9908-9913.
    • (2009) Proc. Natl Acad. Sci. U S A. , vol.106 , pp. 9908-9913
    • Michalska, J.1    Zauber, H.2    Buchanan, B.B.3    Cejudo, F.J.4    Geigenberger, P.5
  • 30
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 32
    • 78650996746 scopus 로고    scopus 로고
    • Targeting mitochondrial metabolism and machinery as a means to enhance photosynthesis
    • Nunes-Nesi, A., Araujo, W.L., and Fernie, A.R. (2011). Targeting mitochondrial metabolism and machinery as a means to enhance photosynthesis. Plant Physiol. 155, 101-107.
    • (2011) Plant Physiol. , vol.155 , pp. 101-107
    • Nunes-Nesi, A.1    Araujo, W.L.2    Fernie, A.R.3
  • 34
    • 0033890234 scopus 로고    scopus 로고
    • Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase
    • Pettersson, H., Olsson, P., Bülow, L., and Pettersson, G. (2000) Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase. Eur. J. Biochem. 267, 5041-5046.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5041-5046
    • Pettersson, H.1    Olsson, P.2    Bülow, L.3    Pettersson, G.4
  • 35
    • 33644802667 scopus 로고    scopus 로고
    • Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination
    • Pracharoenwattana, I., Cornah, J.E., and Smith, S.M. (2005). Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination. Plant Cell. 17, 2037-2048.
    • (2005) Plant Cell. , vol.17 , pp. 2037-2048
    • Pracharoenwattana, I.1    Cornah, J.E.2    Smith, S.M.3
  • 36
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007). Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906.
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 37
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution
    • Remington, S., Wiegand, G., and Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158, 111-152.
    • (1982) J. Mol. Biol. , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 38
    • 0026485965 scopus 로고
    • Structure and mechanism of citrate synthase
    • Remington, S.J. (1992). Structure and mechanism of citrate synthase. Curr. Top. Cell. Regul. 33, 209-229.
    • (1992) Curr. Top. Cell. Regul. , vol.33 , pp. 209-229
    • Remington, S.J.1
  • 39
    • 84855358670 scopus 로고    scopus 로고
    • Reduction-oxidation network for flexible adjustment of cellular metabolism in photoautotrophic cells
    • Scheibe, R., and Dietz, K.J. (2012). Reduction-oxidation network for flexible adjustment of cellular metabolism in photoautotrophic cells. Plant Cell Environ. 35, 202-216.
    • (2012) Plant Cell Environ. , vol.35 , pp. 202-216
    • Scheibe, R.1    Dietz, K.J.2
  • 40
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann, P., and Buchanan, B.B. (2008). The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxidants & Redox Signaling. 10, 1235-1274.
    • (2008) Antioxidants & Redox Signaling. , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 42
    • 0001647511 scopus 로고
    • Citrate condensing enzyme of pigeon breast muscle and moth flight muscle
    • Srere, P.A., Gonen, L., and Brazil, H. (1963). Citrate condensing enzyme of pigeon breast muscle and moth flight muscle. Acta Chem. Scand. 17, 129-134.
    • (1963) Acta Chem. Scand. , vol.17 , pp. 129-134
    • Srere, P.A.1    Gonen, L.2    Brazil, H.3
  • 43
    • 6844226210 scopus 로고    scopus 로고
    • Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: Paradoxical differences in redox-sensitivity as compared with the animal enzyme
    • Stevens, F.J., Li, A.D., Lateef, S.S., and Anderson, L.E. (1997). Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: paradoxical differences in redox-sensitivity as compared with the animal enzyme. Photosynthesis Research. 54, 185-197.
    • (1997) Photosynthesis Research. , vol.54 , pp. 185-197
    • Stevens, F.J.1    Li, A.D.2    Lateef, S.S.3    Anderson, L.E.4
  • 44
    • 84864403917 scopus 로고    scopus 로고
    • Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3
    • Tran, H.T., Nimick, M., Uhrig, R.G., Templeton, G., Morrice, N., Gourlay, R., DeLong, A., and Moorhead, G.B. (2012). Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3. Plant J. 71, 263-272.
    • (2012) Plant J. , vol.71 , pp. 263-272
    • Tran, H.T.1    Nimick, M.2    Uhrig, R.G.3    Templeton, G.4    Morrice, N.5    Gourlay, R.6    Delong, A.7    Moorhead, G.B.8
  • 45
    • 0031588912 scopus 로고    scopus 로고
    • Changes in the redox state of the alternative oxidase regulatory sulfhydryl/disulfide system during mitochondrial isolation: Implications for inferences of activity in vivo
    • Umbach, A.L., Siedow, J.N. (1997). Changes in the redox state of the alternative oxidase regulatory sulfhydryl/disulfide system during mitochondrial isolation: implications for inferences of activity in vivo. Plant Science. 123, 19-28.
    • (1997) Plant Science. , vol.123 , pp. 19-28
    • Umbach, A.L.1    Siedow, J.N.2
  • 46
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq, L., Vignols, F., Jacquot, J.P., Chartier, Y., and Meyer, Y. (1999). In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J. Biol. Chem. 274, 19714-19722.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Chartier, Y.4    Meyer, Y.5
  • 47
    • 0018779501 scopus 로고
    • Crystal-structure analysis of the tetragonal crystal form and preliminary molecular model of pig-heart citrate synthase
    • Wiegand, G., Kukla, D., Scholze, H., Jones, T.A., and Huber, R. (1979). Crystal-structure analysis of the tetragonal crystal form and preliminary molecular model of pig-heart citrate synthase. Eur. J. Biochem. 93, 41-50.
    • (1979) Eur. J. Biochem. , vol.93 , pp. 41-50
    • Wiegand, G.1    Kukla, D.2    Scholze, H.3    Jones, T.A.4    Huber, R.5
  • 48
    • 0021590971 scopus 로고
    • Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A
    • Wiegand, G., Remington, S., Deisenhofer, J., and Huber, R. (1984). Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A. J. Mol. Biol. 174, 205-219.
    • (1984) J. Mol. Biol. , vol.174 , pp. 205-219
    • Wiegand, G.1    Remington, S.2    Deisenhofer, J.3    Huber, R.4
  • 49
    • 36549031664 scopus 로고    scopus 로고
    • Identification of intra-and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis
    • Winger, A.M., Taylor, N.L., Heazlewood, J.L., Day, D.A., and Millar, A.H. (2007). Identification of intra-and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis. Proteomics. 7, 4158-4170.
    • (2007) Proteomics. , vol.7 , pp. 4158-4170
    • Winger, A.M.1    Taylor, N.L.2    Heazlewood, J.L.3    Day, D.A.4    Millar, A.H.5
  • 50
  • 51
    • 84878846165 scopus 로고    scopus 로고
    • Systematic exploration of thioredoxin target proteins in plant mitochondria
    • Yoshida, K., Noguchi, K., Motohashi, K., and Hisabori, T. (2013). Systematic exploration of thioredoxin target proteins in plant mitochondria. Plant Cell Physiol. 54, 875-892.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 875-892
    • Yoshida, K.1    Noguchi, K.2    Motohashi, K.3    Hisabori, T.4
  • 52
    • 13444264729 scopus 로고    scopus 로고
    • Genevestigator. Arabidopsis microarray database and analysis toolbox
    • Zimmermann, P., Hirsch-Hoffmann, M., Hennig, L., and Gruissem, W. (2004). GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136, 2621-2632.
    • (2004) Plant Physiol. , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.