메뉴 건너뛰기




Volumn 119, Issue 3, 1998, Pages 493-503

Glyceraldehyde-3-phosphate dehydrogenase from Tetrahymena pyriformis: Enzyme purification and characterization of a gapC gene with primitive eukaryotic features

Author keywords

cDNA; Chromatofocusing; Ciliates; gapC; Glyceraldehyde 3 phosphate dehydrogenase; Glycolysis; Protist evolution; RT PCR; Tetrahymena pyriformis

Indexed keywords

COMPLEMENTARY DNA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

EID: 0031927301     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(98)00010-8     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 0005650644 scopus 로고    scopus 로고
    • Que savons nous de l'histoire évolutive des eucaryotes? De la diversification des protistes à la radiation des multicellulaires
    • Adoutte A, Germont A, Leguyader H, Philippe H. Que savons nous de l'histoire évolutive des eucaryotes? De la diversification des protistes à la radiation des multicellulaires. Medecine/Sciences 1996;12:1-17.
    • (1996) Medecine/Sciences , vol.12 , pp. 1-17
    • Adoutte, A.1    Germont, A.2    Leguyader, H.3    Philippe, H.4
  • 2
    • 0029069222 scopus 로고
    • Genetic code deviation in the ciliates: Evidence for multiple and independent events
    • Baroin Tourancheau A, Tsao N, Klobutcher LA, Pearlman RE, Adoutte A. Genetic code deviation in the ciliates: evidence for multiple and independent events. EMBO J 1995;14:3262-7.
    • (1995) EMBO J , vol.14 , pp. 3262-3267
    • Baroin Tourancheau, A.1    Tsao, N.2    Klobutcher, L.A.3    Pearlman, R.E.4    Adoutte, A.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 0027145102 scopus 로고
    • Ringdom protozoa and its 18 phyla
    • Cavalier-Smith T. Ringdom protozoa and its 18 phyla. Microbiol Rev 1993;57:953-94.
    • (1993) Microbiol Rev , vol.57 , pp. 953-994
    • Cavalier-Smith, T.1
  • 5
    • 0002219704 scopus 로고
    • The chimeric nature of nuclear genomes and the antiquity of introns as demonstrated by GADPH gene system
    • Go M, Schimmel P, editors. Amsterdam: Elsevier
    • Cerff R. The chimeric nature of nuclear genomes and the antiquity of introns as demonstrated by GADPH gene system. In: Go M, Schimmel P, editors. Tracing Biological Evolution in Protein and Gene Structures. Amsterdam: Elsevier, 1995:205-27.
    • (1995) Tracing Biological Evolution in Protein and Gene Structures , pp. 205-227
    • Cerff, R.1
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chlorophorm extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chlorophorm extraction. Anal Biochem 1987;162:156-9.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0013770850 scopus 로고
    • The isolation and specific activity of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • Ferdinand W. The isolation and specific activity of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biochem J 1964;92:578-85.
    • (1964) Biochem J , vol.92 , pp. 578-585
    • Ferdinand, W.1
  • 9
    • 63849332835 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase
    • Boyer PD, editor. New York: Academic Press
    • Harris JI, Waters M. Glyceraldehyde-3-phosphate dehydrogenase. In: Boyer PD, editor. The Enzymes, 3rd. New York: Academic Press, 1976:1-43.
    • (1976) The Enzymes, 3rd , pp. 1-43
    • Harris, J.I.1    Waters, M.2
  • 10
    • 0029879951 scopus 로고    scopus 로고
    • A non-canonical genetic code in an early divergent eukaryotic lineage
    • Keeling PL, Doolittle WF. A non-canonical genetic code in an early divergent eukaryotic lineage. EMBO J 1996;15:2285-90.
    • (1996) EMBO J , vol.15 , pp. 2285-2290
    • Keeling, P.L.1    Doolittle, W.F.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis
    • Markos A, Miretsky A, Müller M. A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis. J Mol Evol 1993;37:631-43.
    • (1993) J Mol Evol , vol.37 , pp. 631-643
    • Markos, A.1    Miretsky, A.2    Müller, M.3
  • 13
    • 0001291049 scopus 로고
    • Occurrence of phosphorylating and non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenases in photosynthetic organisms
    • Mateos MI, Serrano A. Occurrence of phosphorylating and non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenases in photosynthetic organisms. Plant Sci 1992;84:163-70.
    • (1992) Plant Sci , vol.84 , pp. 163-170
    • Mateos, M.I.1    Serrano, A.2
  • 14
    • 0021753882 scopus 로고
    • Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties
    • Misset O, Opperdoes FR. Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties. Eur J Biochem 1984;144:475-83.
    • (1984) Eur J Biochem , vol.144 , pp. 475-483
    • Misset, O.1    Opperdoes, F.R.2
  • 15
    • 0028231010 scopus 로고
    • The DNA of ciliated protozoa
    • Prescott DM. The DNA of ciliated protozoa. Microbiol Rev 1994;58:233-67.
    • (1994) Microbiol Rev , vol.58 , pp. 233-267
    • Prescott, D.M.1
  • 16
    • 0027262214 scopus 로고
    • Characterization of the glyceraldehyde-3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis
    • Prüb B, Meyer H, Holldorf AW. Characterization of the glyceraldehyde-3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis. Arch Microbiol 1993;160:5-11.
    • (1993) Arch Microbiol , vol.160 , pp. 5-11
    • Prüb, B.1    Meyer, H.2    Holldorf, A.W.3
  • 17
    • 0018794715 scopus 로고
    • Characterization of preribosomal ribonucleoprotein particles from Tetrahymena pyriformis
    • Rodrigues Pousada C, Cyrne ML, Hayes DH. Characterization of preribosomal ribonucleoprotein particles from Tetrahymena pyriformis. Eur J Biochem 1979;102:389-97.
    • (1979) Eur J Biochem , vol.102 , pp. 389-397
    • Rodrigues Pousada, C.1    Cyrne, M.L.2    Hayes, D.H.3
  • 18
    • 0030292470 scopus 로고    scopus 로고
    • Evidence for the heterolobosea from phylogenetic analysis of genes encoding glyceraldehyde-3-phosphate dehydrogenase
    • Roger AJ, Smith MW, Doolittle RF, Doolittle WF. Evidence for the heterolobosea from phylogenetic analysis of genes encoding glyceraldehyde-3-phosphate dehydrogenase. J Euk Microbiol 1996;43:475-85.
    • (1996) J Euk Microbiol , vol.43 , pp. 475-485
    • Roger, A.J.1    Smith, M.W.2    Doolittle, R.F.3    Doolittle, W.F.4
  • 19
    • 0030197949 scopus 로고    scopus 로고
    • Primary structure and phylogenetic relationships of glyceraldehyde-3-phosphate dehydrogenase genes of free-living and parasitic diplomonads flagellates
    • Rozario C, Morin L, Roger AJ, Smith MW, Müller M. Primary structure and phylogenetic relationships of glyceraldehyde-3-phosphate dehydrogenase genes of free-living and parasitic diplomonads flagellates. J Euk Microbiol 1996;43:330-40.
    • (1996) J Euk Microbiol , vol.43 , pp. 330-340
    • Rozario, C.1    Morin, L.2    Roger, A.J.3    Smith, M.W.4    Müller, M.5
  • 21
    • 0028151813 scopus 로고
    • Molecular phylogeny of eukaryotes
    • Schlegel M. Molecular phylogeny of eukaryotes. Tree 1994;9:330-5.
    • (1994) Tree , vol.9 , pp. 330-335
    • Schlegel, M.1
  • 22
    • 0026608941 scopus 로고
    • Phosphonate biosynthesis: Molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli
    • Seidel HM, Pompliano DL, Knowless JR. Phosphonate biosynthesis: molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli. Biochemistry 1992;31:2598-608.
    • (1992) Biochemistry , vol.31 , pp. 2598-2608
    • Seidel, H.M.1    Pompliano, D.L.2    Knowless, J.R.3
  • 23
    • 0022470335 scopus 로고
    • Characterization of cyanobacterial ferredoxin-NADP oxidoreductase molecular heterogeneity using chromatofocusing
    • Serrano A. Characterization of cyanobacterial ferredoxin-NADP oxidoreductase molecular heterogeneity using chromatofocusing. Anal Biochem 1986;154:441-4.
    • (1986) Anal Biochem , vol.154 , pp. 441-444
    • Serrano, A.1
  • 24
    • 0026350705 scopus 로고
    • Differential regulation by trophic conditions of phosphorylating and non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenases in Chlorella fusca
    • Serrano A, Mateos MI, Losada M. Differential regulation by trophic conditions of phosphorylating and non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenases in Chlorella fusca. Biochem Biophys Res Commun 1991;181:1077-83.
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 1077-1083
    • Serrano, A.1    Mateos, M.I.2    Losada, M.3
  • 25
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri A, Mougin A, Corbier C, Wonacott A, Branlant G. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry 1989;28:2586-92.
    • (1989) Biochemistry , vol.28 , pp. 2586-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.4    Branlant, G.5
  • 26
    • 0028872557 scopus 로고
    • Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis
    • Soukri A, Valverde F, Hand N, Elkebbaj MS, Serrano A. Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis. Biochim Biophys Acta 1995;1243:161-8.
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 161-168
    • Soukri, A.1    Valverde, F.2    Hand, N.3    Elkebbaj, M.S.4    Serrano, A.5
  • 27
    • 0030021049 scopus 로고    scopus 로고
    • Evidence for a post-translational covalent modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating jerboa (Jaculus orientalis)
    • Soukri A, Hand N, Valverde F, Elkebbaj MS, Serrano A. Evidence for a post-translational covalent modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating jerboa (Jaculus orientalis). Biochim Biophys Acta 1996;1292:177-87.
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 177-187
    • Soukri, A.1    Hand, N.2    Valverde, F.3    Elkebbaj, M.S.4    Serrano, A.5
  • 28
    • 0000432721 scopus 로고
    • Blue-dextran Sepharose: An affinity column for the dinucleotide fold in proteins
    • Thompson ST, Cass KH, Stellwagen E. Blue-dextran Sepharose: an affinity column for the dinucleotide fold in proteins. Proc Natl Acad Sci USA 1975;72:669-72.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 669-672
    • Thompson, S.T.1    Cass, K.H.2    Stellwagen, E.3
  • 29
    • 12044258111 scopus 로고
    • Tetrahymena: A model for growth, cell cycle and nutritional studies, with biotechnological potential
    • Wheatley DN, Rasmussen L, Tiedtke A. Tetrahymena: a model for growth, cell cycle and nutritional studies, with biotechnological potential. BioEssays 1994;16:367-72.
    • (1994) BioEssays , vol.16 , pp. 367-372
    • Wheatley, D.N.1    Rasmussen, L.2    Tiedtke, A.3
  • 30
    • 0015114886 scopus 로고
    • Synchrony in cell division and growth
    • Zeuthen E. Synchrony in cell division and growth. Exp Cell Res 1971;68:49-60.
    • (1971) Exp Cell Res , vol.68 , pp. 49-60
    • Zeuthen, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.