메뉴 건너뛰기




Volumn 36, Issue 5, 1998, Pages 691-698

NAD+-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Characterization of two closely related subunits

Author keywords

Arabidopsis thaliana; NAD+ dependent isocitrate dehydrogenase

Indexed keywords

AMINO ACID SEQUENCE; COMPLEMENTARY DNA; DNA STRUCTURE; ESCHERICHIA COLI; FUNGAL MUTANT; MUTATIONAL ANALYSIS; SACCHAROMYCES CEREVISIAE; SOUTHERN BLOTTING;

EID: 0032033378     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005923410940     Document Type: Article
Times cited : (16)

References (37)
  • 2
    • 0028143494 scopus 로고
    • Pyruvate dehydrogenase multienzyme complex. Characterization of assembly intermediates by sedimentation velocity analysis
    • Behal RH, DeBuysere MS, Demeler B, Hansen JC, Olson MS: Pyruvate dehydrogenase multienzyme complex. Characterization of assembly intermediates by sedimentation velocity analysis. J Biol Chem 269: 31372-31377 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 31372-31377
    • Behal, R.H.1    DeBuysere, M.S.2    Demeler, B.3    Hansen, J.C.4    Olson, M.S.5
  • 3
    • 0025841651 scopus 로고
    • +-dependent isocitrate dehydrogenase: Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae
    • +-dependent isocitrate dehydrogenase: cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. J Biol Chem 266: 22199-22205 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 22199-22205
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 4
    • 0026784538 scopus 로고
    • +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae
    • +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae. J Biol Chem 267: 16417-16423 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 16417-16423
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 5
    • 0027432796 scopus 로고
    • +-isocitrate dehydrogenase with altered isocitrate binding sites: Contribution of IDH1 and IDH2 subunits to regulation and catalysis
    • +-isocitrate dehydrogenase with altered isocitrate binding sites: contribution of IDH1 and IDH2 subunits to regulation and catalysis. Biochemistry 32: 9323-9328 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9323-9328
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 6
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum G, Bohni PC, Schatz G: Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J Biol Chem 257: 13028-13033 (1982).
    • (1982) J Biol Chem , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 7
    • 0000228203 scopus 로고
    • Dayhoff MO (eds) National Biomedical Research Foundation, Washington
    • Dayhoff MO, Schwartz RM, Orcutt BC: In Dayhoff MO (eds) Atlas of Protein Sequence and Structure, Vol. 5, Suppl. 3. pp. 345-352. National Biomedical Research Foundation, Washington (1978).
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.3 SUPPL. , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 8
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle JJ, Doyle, JL: Isolation of plant DNA from fresh tissue. Focus 12: 13-15 (1990).
    • (1990) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 9
    • 0021099628 scopus 로고
    • Separation, recombination, and characterization of dissimilar subunits of the DPN-dependent isocitrate dehydrogenase from pig heart
    • Ehrlich RS, Colman RF: Separation, recombination, and characterization of dissimilar subunits of the DPN-dependent isocitrate dehydrogenase from pig heart. J Biol Chem 258: 7079-7086 (1983).
    • (1983) J Biol Chem , vol.258 , pp. 7079-7086
    • Ehrlich, R.S.1    Colman, R.F.2
  • 10
    • 0021148480 scopus 로고
    • The role of dissimilar subunits of NAD-specific isocitrate dehydrogenase from pig heart. Evaluation using affinity labeling
    • Ehrlich RS, Colman RF: The role of dissimilar subunits of NAD-specific isocitrate dehydrogenase from pig heart. Evaluation using affinity labeling. J Biol Chem 259: 11936-11942 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 11936-11942
    • Ehrlich, R.S.1    Colman, R.F.2
  • 11
    • 0025836541 scopus 로고
    • Direct in-gel hybridization, without blotting, using nick-translated cloned DNA probe
    • Etesham NZ, Hasnain SE: Direct in-gel hybridization, without blotting, using nick-translated cloned DNA probe. BioTechniques 11: 718-721 (1991).
    • (1991) BioTechniques , vol.11 , pp. 718-721
    • Etesham, N.Z.1    Hasnain, S.E.2
  • 12
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J: Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39: 783-791 (1985).
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 13
    • 0021010725 scopus 로고
    • Import of polypeptides into isolated yeast mitochondria
    • Gasser SM: Import of polypeptides into isolated yeast mitochondria. Meth Enzymol 97: 329-336 (1983).
    • (1983) Meth Enzymol , vol.97 , pp. 329-336
    • Gasser, S.M.1
  • 14
    • 0020479718 scopus 로고
    • Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria
    • Gasser SM, Daum G, Schatz G: Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria. J Biol Chem 257: 13034-13041 (1982).
    • (1982) J Biol Chem , vol.257 , pp. 13034-13041
    • Gasser, S.M.1    Daum, G.2    Schatz, G.3
  • 15
    • 0022895277 scopus 로고
    • Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c Reductase
    • Haitl FU, Schmidt B, Wachter E, Weiss H, Neupert W: Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c Reductase. Cell 47: 939-951 (1986).
    • (1986) Cell , vol.47 , pp. 939-951
    • Haitl, F.U.1    Schmidt, B.2    Wachter, E.3    Weiss, H.4    Neupert, W.5
  • 16
    • 0027310324 scopus 로고
    • Function and expression of yeast mitochondrial NAD- And NADP-specific isocitrate dehydrogenases
    • Haselbeck RJ, McAlister-Henn L: Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases. J Biol Chem 268: 12116-12122 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 12116-12122
    • Haselbeck, R.J.1    McAlister-Henn, L.2
  • 17
    • 0002726601 scopus 로고
    • Regulation of mitochondrial function and biogenesis in cucumber cotyledons during early seedling growth
    • Hill SA, Grof CPL, Bryce JH, Leaver CJ: Regulation of mitochondrial function and biogenesis in cucumber cotyledons during early seedling growth. Plant Physiol 99: 60-66 (1992).
    • (1992) Plant Physiol , vol.99 , pp. 60-66
    • Hill, S.A.1    Grof, C.P.L.2    Bryce, J.H.3    Leaver, C.J.4
  • 18
    • 0025004005 scopus 로고
    • Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase
    • Huang YC, Colman RF: Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase. Biochemistry 29: 8266-8273 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8266-8273
    • Huang, Y.C.1    Colman, R.F.2
  • 22
    • 0029015096 scopus 로고
    • +-specific isocitrate dehydrogenase α subunit and structural comparison with its isoenzymes from different species
    • +-specific isocitrate dehydrogenase α subunit and structural comparison with its isoenzymes from different species. Biochem J 308: 63-68 (1995).
    • (1995) Biochem J , vol.308 , pp. 63-68
    • Kim, Y.O.1    Oh, I.U.2    Park, H.S.3    Jeng, J.4    Song, B.J.5    Huh, T.L.6
  • 23
    • 0002564432 scopus 로고
    • +-linked isocitrate dehydrogenase: Isolation, purification, and characterization of the protein from pea mitochondria
    • +-linked isocitrate dehydrogenase: isolation, purification, and characterization of the protein from pea mitochondria. Plant Physiol 100: 69-75 (1992).
    • (1992) Plant Physiol , vol.100 , pp. 69-75
    • McIntosh, C.A.1    Oliver, D.J.2
  • 24
    • 0001690709 scopus 로고
    • Metabolite oxidation and transport in mitochondria of endosperm from germinating castor bean
    • Millhouse J, Wiskich JT, Beevers H: Metabolite oxidation and transport in mitochondria of endosperm from germinating castor bean. Aust J Plant Phys 10: 167-177 (1983).
    • (1983) Aust J Plant Phys , vol.10 , pp. 167-177
    • Millhouse, J.1    Wiskich, J.T.2    Beevers, H.3
  • 28
    • 0019332922 scopus 로고
    • Chemical characterization of distinct subunits of pig heart DPN-specific isocitrate dehydrogenase
    • Ramachandran N, Colman RF: Chemical characterization of distinct subunits of pig heart DPN-specific isocitrate dehydrogenase. J Biol Chem 255: 8859-8864 (1980).
    • (1980) J Biol Chem , vol.255 , pp. 8859-8864
    • Ramachandran, N.1    Colman, R.F.2
  • 29
    • 0018266783 scopus 로고
    • Nicotinamide adenine dinucleotide dependent isocitrate dehydrogenase from beef heart: Subunit heterogeneity and enzyme dissociation
    • Rushbrook JI, Harvey RA: Nicotinamide adenine dinucleotide dependent isocitrate dehydrogenase from beef heart: subunit heterogeneity and enzyme dissociation. Biochemistry 17: 5339-5346 (1978).
    • (1978) Biochemistry , vol.17 , pp. 5339-5346
    • Rushbrook, J.I.1    Harvey, R.A.2
  • 30
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M: The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425 (1987).
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 32
    • 0027442820 scopus 로고
    • Structure of isocitrate dehydrogenase with a-ketoglutarate at 2.7-È resolution: Conformational changes induced by decarboxcylation of isocitrate
    • StoddardBL, Koshland DE, Jr.: Structure of isocitrate dehydrogenase with a-ketoglutarate at 2.7-È resolution: conformational changes induced by decarboxcylation of isocitrate. Biochemistry 32: 9317-9322 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9317-9322
    • Stoddard, B.L.1    Koshland Jr., D.E.2
  • 33
    • 0027494760 scopus 로고
    • Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-È resolution: A pseudo-Michaelis ternary complex
    • Stoddard BL, Dean A, Koshland DE, Jr.: Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-È resolution: a pseudo-Michaelis ternary complex. Biochemistry 32: 9310-9316 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9310-9316
    • Stoddard, B.L.1    Dean, A.2    Koshland Jr., D.E.3
  • 35
    • 0023645302 scopus 로고
    • The inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness PE, Koshland DE Jr: The inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J Biol Chem 262: 10422-10425 (1987).
    • (1987) J Biol Chem , vol.262 , pp. 10422-10425
    • Thorsness, P.E.1    Koshland Jr., D.E.2
  • 37
    • 0029971335 scopus 로고    scopus 로고
    • Assembly and function of a cytosolic form of NADH-specific isocitrate dehydrogenase in yeast
    • Zhao W-N, McAlister-Henn L: Assembly and function of a cytosolic form of NADH-specific isocitrate dehydrogenase in yeast. J Biol Chem 271: 10347-10352 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 10347-10352
    • Zhao, W.-N.1    McAlister-Henn, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.