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Volumn 172, Issue 2, 2016, Pages 901-912

D-lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CYTOCHROME C; LACTATE DEHYDROGENASE; LACTIC ACID; METHYLGLYOXAL; PYRUVIC ACID;

EID: 84989337916     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.16.01174     Document Type: Article
Times cited : (48)

References (46)
  • 3
    • 0026672186 scopus 로고
    • Affinity purification of cytochrome c reductase from potato mitochondria
    • Braun HP, Schmitz UK (1992) Affinity purification of cytochrome c reductase from potato mitochondria. Eur J Biochem 208: 761-767
    • (1992) Eur J Biochem , vol.208 , pp. 761-767
    • Braun, H.P.1    Schmitz, U.K.2
  • 4
    • 0026646597 scopus 로고
    • The effect of antimycin A on mouse liver inner mitochondrial membrane channel activity
    • Campo ML, Kinnally KW, Tedeschi H (1992) The effect of antimycin A on mouse liver inner mitochondrial membrane channel activity. J Biol Chem 267: 8123-8127
    • (1992) J Biol Chem , vol.267 , pp. 8123-8127
    • Campo, M.L.1    Kinnally, K.W.2    Tedeschi, H.3
  • 5
    • 77950347534 scopus 로고    scopus 로고
    • The plastid isoform of triose phosphate isomerase is required for the postgerminative transition from heterotrophic to autotrophic growth in Arabidopsis
    • Chen M, Thelen JJ (2010) The plastid isoform of triose phosphate isomerase is required for the postgerminative transition from heterotrophic to autotrophic growth in Arabidopsis. Plant Cell 22: 77-90
    • (2010) Plant Cell , vol.22 , pp. 77-90
    • Chen, M.1    Thelen, J.J.2
  • 6
    • 70449531397 scopus 로고    scopus 로고
    • Evolutionary history of D-lactate dehydrogenases: A phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family
    • Cristescu ME, Egbosimba EE (2009) Evolutionary history of D-lactate dehydrogenases: a phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family. J Mol Evol 69: 276-287
    • (2009) J Mol Evol , vol.69 , pp. 276-287
    • Cristescu, M.E.1    Egbosimba, E.E.2
  • 8
    • 69949120428 scopus 로고    scopus 로고
    • Two D-2- hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways
    • Engqvist M, Drincovich MF, Flügge UI, Maurino VG (2009) Two D-2- hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways. J Biol Chem 284: 25026-25037
    • (2009) J Biol Chem , vol.284 , pp. 25026-25037
    • Engqvist, M.1    Drincovich, M.F.2    Flügge, U.I.3    Maurino, V.G.4
  • 9
    • 84926501050 scopus 로고    scopus 로고
    • Mito Fates: Improved prediction of mitochondrial targeting sequences and their cleavage sites
    • Fukasawa Y, Tsuji J, Fu SC, Tomii K, Horton P, Imai K (2015) Mito Fates: improved prediction of mitochondrial targeting sequences and their cleavage sites. Mol Cell Proteomics 14: 1113-1126
    • (2015) Mol Cell Proteomics , vol.14 , pp. 1113-1126
    • Fukasawa, Y.1    Tsuji, J.2    Fu, S.C.3    Tomii, K.4    Horton, P.5    Imai, K.6
  • 10
    • 84895543893 scopus 로고    scopus 로고
    • The ins and outs of the intermembrane space: Diverse mechanisms and evolutionary rewiring of mitochondrial protein import routes
    • Hewitt VL, Gabriel K, Traven A (2014) The ins and outs of the intermembrane space: diverse mechanisms and evolutionary rewiring of mitochondrial protein import routes. Biochim Biophys Acta 1840: 1246-1253
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 1246-1253
    • Hewitt, V.L.1    Gabriel, K.2    Traven, A.3
  • 11
    • 0000207681 scopus 로고
    • TMbase: A database of membrane spanning proteins segments
    • Hofmann K, Stoffel W (1993) TMbase: a database of membrane spanning proteins segments. Biol Chem Hoppe Seyler 374: 166
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 12
    • 84861790604 scopus 로고    scopus 로고
    • Methylglyoxal-induced stomatal closure accompanied by peroxidasemediated ROS production in Arabidopsis
    • Hoque TS, Uraji M, Ye W, Hossain MA, Nakamura Y, Murata Y (2012) Methylglyoxal-induced stomatal closure accompanied by peroxidasemediated ROS production in Arabidopsis. J Plant Physiol 169: 979-986
    • (2012) J Plant Physiol , vol.169 , pp. 979-986
    • Hoque, T.S.1    Uraji, M.2    Ye, W.3    Hossain, M.A.4    Nakamura, Y.5    Murata, Y.6
  • 13
    • 4544290279 scopus 로고    scopus 로고
    • Electron acquisition system constructed from an NAD-independent D-lactate dehydrogenase and cytochrome c2 in Rhodopseudomonas palustris No. 7
    • Horikiri S, Aizawa Y, Kai T, Amachi S, Shinoyama H, Fujii T (2004) Electron acquisition system constructed from an NAD-independent D-lactate dehydrogenase and cytochrome c2 in Rhodopseudomonas palustris No. 7. Biosci Biotechnol Biochem 68: 516-522
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 516-522
    • Horikiri, S.1    Aizawa, Y.2    Kai, T.3    Amachi, S.4    Shinoyama, H.5    Fujii, T.6
  • 14
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: Chemistry, biochemistry, toxicology and biological implications
    • Kalapos MP (1999) Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol Lett 110: 145-175
    • (1999) Toxicol Lett , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 15
    • 23144452690 scopus 로고    scopus 로고
    • Preparation of leaf mitochondria from Arabidopsis thaliana
    • Keech O, Dizengremel P, Gardestrom P (2005) Preparation of leaf mitochondria from Arabidopsis thaliana. Physiol Plant 124: 403-409
    • (2005) Physiol Plant , vol.124 , pp. 403-409
    • Keech, O.1    Dizengremel, P.2    Gardestrom, P.3
  • 16
    • 80053594838 scopus 로고    scopus 로고
    • Defining the protein complex proteome of plant mitochondria
    • Klodmann J, Senkler M, Rode C, Braun HP (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
  • 17
    • 77953226426 scopus 로고    scopus 로고
    • Internal architecture of mitochondrial complex I from Arabidopsis thaliana
    • Klodmann J, Sunderhaus S, Nimtz M, Jänsch L, Braun HP (2010) Internal architecture of mitochondrial complex I from Arabidopsis thaliana. Plant Cell 22: 797-810
    • (2010) Plant Cell , vol.22 , pp. 797-810
    • Klodmann, J.1    Sunderhaus, S.2    Nimtz, M.3    Jänsch, L.4    Braun, H.P.5
  • 19
    • 0027210771 scopus 로고
    • Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase
    • Lodi T, Ferrero I (1993) Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase. Mol Gen Genet 238: 315-324
    • (1993) Mol Gen Genet , vol.238 , pp. 315-324
    • Lodi, T.1    Ferrero, I.2
  • 20
    • 0027942216 scopus 로고
    • Carbon catabolite repression in Kluyveromyces lactis: Isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase
    • Lodi T, O’Connor D, Goffrini P, Ferrero I (1994) Carbon catabolite repression in Kluyveromyces lactis: isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase. Mol Gen Genet 244: 622-629
    • (1994) Mol Gen Genet , vol.244 , pp. 622-629
    • Lodi, T.1    O’Connor, D.2    Goffrini, P.3    Ferrero, I.4
  • 21
    • 0141787893 scopus 로고    scopus 로고
    • Mitochondrial and cytosolic calcium dynamics are differentially regulated in plants
    • Logan DC, Knight MR (2003) Mitochondrial and cytosolic calcium dynamics are differentially regulated in plants. Plant Physiol 133: 21-24
    • (2003) Plant Physiol , vol.133 , pp. 21-24
    • Logan, D.C.1    Knight, M.R.2
  • 22
    • 0034029619 scopus 로고    scopus 로고
    • Mitochondria-targeted GFP highlights the heterogeneity of mitochondrial shape, size and movement within living plant cells
    • Logan DC, Leaver CJ (2000) Mitochondria-targeted GFP highlights the heterogeneity of mitochondrial shape, size and movement within living plant cells. J Exp Bot 51: 865-871
    • (2000) J Exp Bot , vol.51 , pp. 865-871
    • Logan, D.C.1    Leaver, C.J.2
  • 23
    • 84872255673 scopus 로고    scopus 로고
    • P AUL: A Gatewaybased vector system for adaptive expression and flexible tagging of proteins in Arabidopsis
    • Lyska D, Engelmann K, Meierhoff K, Westhoff P (2013) p AUL: a Gatewaybased vector system for adaptive expression and flexible tagging of proteins in Arabidopsis. PLo S ONE 8: e53787
    • (2013) PLo S ONE , vol.8 , pp. e53787
    • Lyska, D.1    Engelmann, K.2    Meierhoff, K.3    Westhoff, P.4
  • 24
    • 84970004624 scopus 로고    scopus 로고
    • 2-Hydroxy acids in plant metabolism
    • Maurino VG, Engqvist MK (2015) 2-Hydroxy acids in plant metabolism. The Arabidopsis Book 13: e0182, doi/10.1199/tab.0182
    • (2015) The Arabidopsis Book , vol.13 , pp. e0182
    • Maurino, V.G.1    Engqvist, M.K.2
  • 25
    • 0028939260 scopus 로고
    • Glyoxalase III from Escherichia coli: A single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione
    • Misra K, Banerjee AB, Ray S, Ray M (1995) Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem J 305: 999-1003
    • (1995) Biochem J , vol.305 , pp. 999-1003
    • Misra, K.1    Banerjee, A.B.2    Ray, S.3    Ray, M.4
  • 26
    • 1042278877 scopus 로고    scopus 로고
    • Two separate pathways for D-lactate oxidation by Saccharomyces cerevisiae mitochondria which differ in energy production and carrier involvement
    • Pallotta ML, Valenti D, Iacovino M, Passarella S (2004) Two separate pathways for D-lactate oxidation by Saccharomyces cerevisiae mitochondria which differ in energy production and carrier involvement. Biochim Biophys Acta 1608: 104-113
    • (2004) Biochim Biophys Acta , vol.1608 , pp. 104-113
    • Pallotta, M.L.1    Valenti, D.2    Iacovino, M.3    Passarella, S.4
  • 27
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates: Investigation using a specific assay for methylglyoxal
    • Phillips SA, Thornalley PJ (1993) The formation of methylglyoxal from triose phosphates: investigation using a specific assay for methylglyoxal. Eur J Biochem 212: 101-105
    • (1993) Eur J Biochem , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 28
    • 80052032987 scopus 로고    scopus 로고
    • Gel Map: A novel software tool for building and presenting proteome reference maps
    • Rode C, Senkler M, Klodmann J, Winkelmann T, Braun HP (2011) Gel Map: a novel software tool for building and presenting proteome reference maps. J Proteomics 74: 2214-2219
    • (2011) J Proteomics , vol.74 , pp. 2214-2219
    • Rode, C.1    Senkler, M.2    Klodmann, J.3    Winkelmann, T.4    Braun, H.P.5
  • 31
    • 84901065582 scopus 로고    scopus 로고
    • Respiratory electron transfer pathways in plant mitochondria
    • Schertl P, Braun HP (2014) Respiratory electron transfer pathways in plant mitochondria. Front Plant Sci 5: 163
    • (2014) Front Plant Sci , vol.5 , pp. 163
    • Schertl, P.1    Braun, H.P.2
  • 32
    • 79960209663 scopus 로고    scopus 로고
    • The circularly permuted yellow fluorescent protein cp YFP that has been used as a superoxide probe is highly responsive to p H but not superoxide in mitochondria: Implications for the existence of superoxide ‘flashes
    • Schwarzländer M, Logan DC, Fricker MD, Sweetlove LJ (2011) The circularly permuted yellow fluorescent protein cp YFP that has been used as a superoxide probe is highly responsive to p H but not superoxide in mitochondria: implications for the existence of superoxide ‘flashes.' Biochem J 437: 381-387
    • (2011) Biochem J , vol.437 , pp. 381-387
    • Schwarzländer, M.1    Logan, D.C.2    Fricker, M.D.3    Sweetlove, L.J.4
  • 33
    • 84881308650 scopus 로고    scopus 로고
    • Functional annotation of 2D protein maps: The Gel Map portal
    • Senkler M, Braun HP (2012) Functional annotation of 2D protein maps: the Gel Map portal. Front Plant Sci 3: 87
    • (2012) Front Plant Sci , vol.3 , pp. 87
    • Senkler, M.1    Braun, H.P.2
  • 34
  • 36
    • 0347419281 scopus 로고    scopus 로고
    • Glyoxalase I: Structure, function and a critical role in the enzymatic defence against glycation
    • Thornalley PJ (2003) Glyoxalase I: structure, function and a critical role in the enzymatic defence against glycation. Biochem Soc Trans 31: 1343-1348
    • (2003) Biochem Soc Trans , vol.31 , pp. 1343-1348
    • Thornalley, P.J.1
  • 37
    • 33645011305 scopus 로고    scopus 로고
    • Characterization of transformed Arabidopsis with altered alternative oxidase levels and analysis of effects on reactive oxygen species in tissue
    • Umbach AL, Fiorani F, Siedow JN (2005) Characterization of transformed Arabidopsis with altered alternative oxidase levels and analysis of effects on reactive oxygen species in tissue. Plant Physiol 139: 1806-1820
    • (2005) Plant Physiol , vol.139 , pp. 1806-1820
    • Umbach, A.L.1    Fiorani, F.2    Siedow, J.N.3
  • 39
    • 0021214403 scopus 로고
    • An inhibitor of mitochondrial respiration which binds to cytochrome b and displaces quinone from the iron-sulfur protein of the cytochrome bc1 complex
    • von Jagow G, Ljungdahl PO, Graf P, Ohnishi T, Trumpower BL (1984) An inhibitor of mitochondrial respiration which binds to cytochrome b and displaces quinone from the iron-sulfur protein of the cytochrome bc1 complex. J Biol Chem 259: 6318-6326
    • (1984) J Biol Chem , vol.259 , pp. 6318-6326
    • von Jagow, G.1    Ljungdahl, P.O.2    Graf, P.3    Ohnishi, T.4    Trumpower, B.L.5
  • 41
    • 85027916945 scopus 로고    scopus 로고
    • Cytochrome c, a hub linking energy, redox, stress and signaling pathways in mitochondria and other cell compartments
    • Welchen E, Gonzalez DH (2016) Cytochrome c, a hub linking energy, redox, stress and signaling pathways in mitochondria and other cell compartments. Physiol Plant 157: 310-321
    • (2016) Physiol Plant , vol.157 , pp. 310-321
    • Welchen, E.1    Gonzalez, D.H.2
  • 42
    • 84860794562 scopus 로고    scopus 로고
    • Lack of cytochrome c in Arabidopsis decreases stability of complex IV and modifies redox metabolism without affecting complexes I and III
    • Welchen E, Hildebrandt TM, Lewejohann D, Gonzalez DH, Braun HP (2012) Lack of cytochrome c in Arabidopsis decreases stability of complex IV and modifies redox metabolism without affecting complexes I and III. Biochim Biophys Acta 1817: 990-1001
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 990-1001
    • Welchen, E.1    Hildebrandt, T.M.2    Lewejohann, D.3    Gonzalez, D.H.4    Braun, H.P.5
  • 43
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis: Identification of multiple forms of TOM20
    • Werhahn W, Niemeyer A, Jänsch L, Kruft V, Schmitz UK, Braun H (2001) Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis: identification of multiple forms of TOM20. Plant Physiol 125: 943-954
    • (2001) Plant Physiol , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.6
  • 44
    • 84655163773 scopus 로고    scopus 로고
    • D-Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants
    • Wienstroer J, Engqvist MK, Kunz HH, Flügge UI, Maurino VG (2012) D-Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants. FEBS Lett 586: 36-40
    • (2012) FEBS Lett , vol.586 , pp. 36-40
    • Wienstroer, J.1    Engqvist, M.K.2    Kunz, H.H.3    Flügge, U.I.4    Maurino, V.G.5
  • 46


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