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Volumn 89, Issue 2, 2006, Pages 213-223

Transferring redox regulation properties from sorghum NADP-malate dehydrogenase to Thermus NAD-malate dehydrogenase

Author keywords

Disulfide; Malate dehydrogenase; Redox regulation; Thioredoxin

Indexed keywords

CHIMERIC PROTEIN; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (NADP);

EID: 34249914699     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-006-9094-4     Document Type: Article
Times cited : (8)

References (27)
  • 1
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amman E, Ochs B, Abel K-J (1988) Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amman, E.1    Ochs, B.2    Abel, K.-J.3
  • 3
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light- dependent regulation of activity by thiol oxidation and reduction
    • DOI 10.1016/S0969-2126(99)80058-6
    • Carr P, Verger D, Ashton AR, Ollis D (1999) Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Structure 7:461-475 (Pubitemid 29190479)
    • (1999) Structure , vol.7 , Issue.4 , pp. 461-475
    • Carr, P.D.1    Verger, D.2    Ashton, A.R.3    Ollis, D.L.4
  • 4
    • 4344641295 scopus 로고    scopus 로고
    • Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox regulatory cluster
    • Cazalis R, Chueca A, Sahrawy M, Lopez-Gorge J (2004) Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox regulatory cluster. J Physiol Biochem 60:7-21
    • (2004) J Physiol Biochem , vol.60 , pp. 7-21
    • Cazalis, R.1    Chueca, A.2    Sahrawy, M.3    Lopez-Gorge, J.4
  • 6
    • 0035929368 scopus 로고    scopus 로고
    • Sites of interaction of thioredoxin with sorghum NADP-malate dehydrogenase
    • DOI 10.1016/S0014-5793(01)02860-5, PII S0014579301028605
    • Goyer A, Decottignies P, Issakidis-Bourguet E, Miginiac-Maslow M (2001) Sites of interaction of thioredoxin with sorghum NADP-malate dehydrogenase. FEBS Lett 505:405-408 (Pubitemid 32905486)
    • (2001) FEBS Letters , vol.505 , Issue.3 , pp. 405-408
    • Goyer, A.1    Decottignies, P.2    Issakidis-Bourguet, E.3    Miginiac-Maslow, M.4
  • 7
    • 0000767324 scopus 로고
    • Bi-level disulfide group reduction in the activation of C4 leaf nicotinamide adenine dinucleotide phosphate malate dehydrogenase
    • Hatch MD, Agostino A (1992) Bi-level disulfide group reduction in the activation of C4 leaf nicotinamide adenine dinucleotide phosphate malate dehydrogenase. Plant Physiol 100:360-366
    • (1992) Plant Physiol , vol.100 , pp. 360-366
    • Hatch, M.D.1    Agostino, A.2
  • 8
    • 0034724284 scopus 로고    scopus 로고
    • Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase
    • DOI 10.1021/bi9916731
    • Hirasawa M, Ruelland E, Schepens I, Issakidis-Bourguet E, Miginiac-Maslow M, Knaff DB (2000) Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast NADP-malate dehydrogenase. Biochemistry 39:3344-3350 (Pubitemid 30170004)
    • (2000) Biochemistry , vol.39 , Issue.12 , pp. 3344-3350
    • Hirasawa, M.1    Ruelland, E.2    Schepens, I.3    Issakidis-Bourguet, E.4    Miginiac-Maslow, M.5    Knaff, D.B.6
  • 9
    • 0011786350 scopus 로고
    • Molecular cloning of Thermus flavus malate dehydrogenase gene
    • Iijima S, Uozumi T, Beppu T (1986) Molecular cloning of Thermus flavus malate dehydrogenase gene. Agric Biol Chem 50:589-592
    • (1986) Agric Biol Chem , vol.50 , pp. 589-592
    • Iijima, S.1    Uozumi, T.2    Beppu, T.3
  • 10
    • 0026788107 scopus 로고
    • Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase
    • Issakidis E, Miginiac-Maslow M, Decottignies P, Jacquot JP, Crétin C, Gadal P (1992) Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase. J Biol Chem 267:21577-21583
    • (1992) J Biol Chem , vol.267 , pp. 21577-21583
    • Issakidis, E.1    Miginiac-Maslow, M.2    Decottignies, P.3    Jacquot, J.P.4    Crétin, C.5    Gadal, P.6
  • 11
    • 0027991093 scopus 로고
    • Identification and characterization of the second regulatory disulfide bridge of recombinant sorghum leaf NADP-malate dehydrogenase
    • Issakidis E, Saarinen M, Decottignies P, Jacquot JP, Crétin C, Gadal P, Miginiac-Maslow M (1994) Identification and characterization of the second regulatory disulfide bridge of recombinant sorghum leaf NADP-malate dehydrogenase. J Biol Chem 269:3511-3517
    • (1994) J Biol Chem , vol.269 , pp. 3511-3517
    • Issakidis, E.1    Saarinen, M.2    Decottignies, P.3    Jacquot, J.P.4    Crétin, C.5    Gadal, P.6    Miginiac-Maslow, M.7
  • 13
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ (1993) Determinants of protein thermostability observed in the 1.9-Åcrystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry 32:3913-3922 (Pubitemid 23126979)
    • (1993) Biochemistry , vol.32 , Issue.15 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 14
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14:51-55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 15
    • 0030917877 scopus 로고    scopus 로고
    • The ATP synthase γ subunit provides the primary site of activation of the chloroplast enzyme: Experiments with a chloroplast-like Synechocystis 6803 mutant
    • Krenn BE, Strotmann H, Van Walraven HS, Scholts MJC, Kraayenhof R (1997) The ATP synthase γ subunit provides the primary site of activation of the chloroplast enzyme: experiments with a chloroplast-like Synechocystis 6803 mutant. Biochem J 323:841-845 (Pubitemid 27202357)
    • (1997) Biochemical Journal , vol.323 , Issue.3 , pp. 841-845
    • Krenn, B.E.1    Strotmann, H.2    Van Walraven, H.S.3    Scholts, M.J.C.4    Kraayenhof, R.5
  • 16
    • 0033521039 scopus 로고    scopus 로고
    • Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition
    • Krimm I, Goyer A, Issakidis-Bourguet E, Miginiac-Maslow M, Lancelin JM (1999) Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydogenase provides a structural basis for the relief of auto-inhibition. J Biol Chem 274:34539-34542 (Pubitemid 129509488)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34539-34542
    • Krimm, I.1    Goyer, A.2    Issakidis-Bourguet, E.3    Miginiac-Maslow, M.4    Lancelin, J.-M.5
  • 18
    • 0036320250 scopus 로고    scopus 로고
    • Intrasteric inhibition in redox signalling: Light activation of NADP-malate dehydrogenase
    • DOI 10.1023/A:1016099228450
    • Miginiac-Maslow M, Lancelin JM (2002) Intrasteric inhibition in redox signaling: light activation of NADP-malate dehydrogenase. Photosyn Res 72:1-12 (Pubitemid 34812537)
    • (2002) Photosynthesis Research , vol.72 , Issue.1 , pp. 1-12
    • Miginiac-Maslow, M.1    Lancelin, J.-M.2
  • 19
    • 0023057044 scopus 로고
    • Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity
    • Nishiyama M, Matsubara N, Yamamoto K, Iijima S, Uozumi T, Beppu T (1986) Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. J Biol Chem 261:14178-14183
    • (1986) J Biol Chem , vol.261 , pp. 14178-14183
    • Nishiyama, M.1    Matsubara, N.2    Yamamoto, K.3    Iijima, S.4    Uozumi, T.5    Beppu, T.6
  • 20
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: Activation or relief from inhibition?
    • DOI 10.1016/S1360-1385(99)01391-6, PII S1360138599013916
    • Ruelland E, Miginiac-Maslow M (1999) Regulation of chloroplast enzyme activities by thiol-disulfide interchange with reduced thioredoxin: activation or relief from inhibition? Trends Plant Sci 4:136-141 (Pubitemid 29178028)
    • (1999) Trends in Plant Science , vol.4 , Issue.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 22
    • 0032509509 scopus 로고    scopus 로고
    • The autoinhibition of sorghum NADP malate dehydrogenase is mediated by a C-terminal negative charge
    • DOI 10.1074/jbc.273.50.33482
    • Ruelland E, Johansson K, Decottignies P, Djukic N, Miginiac- Maslow M (1998) The auto-inhibition of sorghum NADPmalate dehydrogenase is mediated by a C-terminal negative charge. J Biol Chem 273:33482-33488 (Pubitemid 29005730)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.50 , pp. 33482-33488
    • Ruelland, E.1    Johansson, K.2    Decottignies, P.3    Djukic, N.4    Miginiac-Maslowi, M.5
  • 25
    • 0034680930 scopus 로고    scopus 로고
    • The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity
    • Schepens I, Ruelland E, Miginiac-Maslow M, Le Maréchal P, Decottignies P (2000b) The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity. J Biol Chem 275:35792-35798
    • (2000) J Biol Chem , vol.275 , pp. 35792-35798
    • Schepens, I.1    Ruelland, E.2    Miginiac-Maslow, M.3    Le Maréchal, P.4    Decottignies, P.5
  • 27
    • 0028168930 scopus 로고
    • Insertion of a "chloroplast-like" regulatory segment responsible for thiol modulation into gamma-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803 by mutagenesis of atpC
    • Werner-Grüne S, Gunkel D, Schumann J, Strotmann H (1994) Insertion of a "chloroplast-like" regulatory segment responsible for thiol modulation into gamma-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803 by mutagenesis of atpC. Mol Gen Genet 244:144-150
    • (1994) Mol Gen Genet , vol.244 , pp. 144-150
    • Werner-Grüne, S.1    Gunkel, D.2    Schumann, J.3    Strotmann, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.