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Volumn 1760, Issue 6, 2006, Pages 913-921

An expanded adenylate kinase gene family in the protozoan parasite Trypanosoma cruzi

Author keywords

Adenylate kinase; Arginine kinase; Chagas' disease; Phosphotransferase; Trypanosoma cruzi

Indexed keywords

ADENYLATE KINASE; ARGININE KINASE; ISOENZYME; MESSENGER RNA; PHOSPHOTRANSFERASE;

EID: 33744817887     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.02.013     Document Type: Article
Times cited : (19)

References (37)
  • 2
    • 0032125880 scopus 로고    scopus 로고
    • Differences in energy metabolism between Trypanosomatidae
    • Tielens A., and Van Hellemond J. Differences in energy metabolism between Trypanosomatidae. Parasitol. Today 14 (1998) 265-271
    • (1998) Parasitol. Today , vol.14 , pp. 265-271
    • Tielens, A.1    Van Hellemond, J.2
  • 3
    • 70349640265 scopus 로고
    • Adenylate kinase
    • Boyer P.D. (Ed), Academic Press, New York
    • Noda L.H. Adenylate kinase. In: Boyer P.D. (Ed). The Enzymes. 3rd ed. vol. 8 (1973), Academic Press, New York 279-305
    • (1973) The Enzymes. 3rd ed. , vol.8 , pp. 279-305
    • Noda, L.H.1
  • 6
    • 0035052706 scopus 로고    scopus 로고
    • Evolution and physiological roles of phosphagen systems
    • Ellington W.R. Evolution and physiological roles of phosphagen systems. Annu. Rev. Physiol. 63 (2001) 289-325
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 289-325
    • Ellington, W.R.1
  • 7
    • 0014930065 scopus 로고
    • Localization of arginine kinase in the cilia of Tetrahymena pyriformis
    • Watts D., and Bannister L. Localization of arginine kinase in the cilia of Tetrahymena pyriformis. Nature 226 (1970) 450-451
    • (1970) Nature , vol.226 , pp. 450-451
    • Watts, D.1    Bannister, L.2
  • 8
    • 0032829684 scopus 로고    scopus 로고
    • Adenylate kinase is tightly bound to axonemes of Tetrahymena cilia
    • Nakamura K., Iitsuka K., and Fuji T. Adenylate kinase is tightly bound to axonemes of Tetrahymena cilia. Comp. Biochem. Physiol., B 124 (1999) 195-199
    • (1999) Comp. Biochem. Physiol., B , vol.124 , pp. 195-199
    • Nakamura, K.1    Iitsuka, K.2    Fuji, T.3
  • 9
    • 0035745332 scopus 로고    scopus 로고
    • ATP-regenerating system in the cilia of Paramecium caudatum
    • Noguchi M., Sawada T., and Akazawa T. ATP-regenerating system in the cilia of Paramecium caudatum. J. Exp. Biol. 204 (2001) 1063-1107
    • (2001) J. Exp. Biol. , vol.204 , pp. 1063-1107
    • Noguchi, M.1    Sawada, T.2    Akazawa, T.3
  • 10
    • 0033984243 scopus 로고    scopus 로고
    • Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
    • Pereira C.A., Alonso G.D., Paveto C., Iribarren A., Cabanas M.L., Torres H.N., and Flawiá M.M. Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites. J. Biol. Chem. 275 (2000) 1495-1501
    • (2000) J. Biol. Chem. , vol.275 , pp. 1495-1501
    • Pereira, C.A.1    Alonso, G.D.2    Paveto, C.3    Iribarren, A.4    Cabanas, M.L.5    Torres, H.N.6    Flawiá, M.M.7
  • 13
    • 0038037716 scopus 로고    scopus 로고
    • Phosphotransfer networks and cellular energetics
    • Dzeja P.P., and Terzic A. Phosphotransfer networks and cellular energetics. J. Exp. Biol. 206 (2003) 2039-2047
    • (2003) J. Exp. Biol. , vol.206 , pp. 2039-2047
    • Dzeja, P.P.1    Terzic, A.2
  • 14
    • 0032518742 scopus 로고    scopus 로고
    • Influence of N-terminal sequence variation on the sorting of major adenylate kinase to the mitochondrial intermembrane space in yeast
    • Bandlow W., Strobel G., and Schricker R. Influence of N-terminal sequence variation on the sorting of major adenylate kinase to the mitochondrial intermembrane space in yeast. Biochem. J. 329 (1998) 359-367
    • (1998) Biochem. J. , vol.329 , pp. 359-367
    • Bandlow, W.1    Strobel, G.2    Schricker, R.3
  • 15
    • 0029937408 scopus 로고    scopus 로고
    • Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family
    • Fukami-Kobayashi K., Nosaka M., Nakazawa A., and Go M. Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family. FEBS Lett. 385 (1996) 214-220
    • (1996) FEBS Lett. , vol.385 , pp. 214-220
    • Fukami-Kobayashi, K.1    Nosaka, M.2    Nakazawa, A.3    Go, M.4
  • 16
    • 0019892206 scopus 로고
    • Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei
    • Opperdoes F., Markos A., and Steiger R. Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei. Mol. Biochem. Parasitol. 4 (1981) 291-309
    • (1981) Mol. Biochem. Parasitol. , vol.4 , pp. 291-309
    • Opperdoes, F.1    Markos, A.2    Steiger, R.3
  • 17
    • 0026662721 scopus 로고
    • Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias
    • Sanchez-Moreno M., Lasztity D., Coppens I., and Opperdoes F. Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias. Mol. Biochem. Parasitol. 54 (1992) 185-199
    • (1992) Mol. Biochem. Parasitol. , vol.54 , pp. 185-199
    • Sanchez-Moreno, M.1    Lasztity, D.2    Coppens, I.3    Opperdoes, F.4
  • 19
    • 3042723185 scopus 로고    scopus 로고
    • Protein targeting of an unusual, evolutionarily conserved adenylate kinase to a eukaryotic flagellum
    • Pullen T.J., Ginger M.L., Gaskell S.J., and Gull K. Protein targeting of an unusual, evolutionarily conserved adenylate kinase to a eukaryotic flagellum. Mol. Biol. Cell 15 (2004) 3257-3265
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3257-3265
    • Pullen, T.J.1    Ginger, M.L.2    Gaskell, S.J.3    Gull, K.4
  • 20
    • 15744385422 scopus 로고    scopus 로고
    • Intracellular positioning of isoforms explains an unusually large adenylate kinase gene family in the parasite Trypanosoma brucei
    • Ginger M.L., Ngazoa E.S., Pereira C.A., Pullen T.J., Kabiri M., Becker K., Gull K., and Steverding D. Intracellular positioning of isoforms explains an unusually large adenylate kinase gene family in the parasite Trypanosoma brucei. J. Biol. Chem. 280 (2005) 11781-11789
    • (2005) J. Biol. Chem. , vol.280 , pp. 11781-11789
    • Ginger, M.L.1    Ngazoa, E.S.2    Pereira, C.A.3    Pullen, T.J.4    Kabiri, M.5    Becker, K.6    Gull, K.7    Steverding, D.8
  • 21
    • 78651145402 scopus 로고
    • Growth and differentiation in Trypanosoma cruzi, Origin of metacyclic trypanosomes in liquid media
    • Camargo E.P. Growth and differentiation in Trypanosoma cruzi, Origin of metacyclic trypanosomes in liquid media. Rev. Inst. Med. Trop. 6 (1964) 93-100
    • (1964) Rev. Inst. Med. Trop. , vol.6 , pp. 93-100
    • Camargo, E.P.1
  • 23
    • 0028933884 scopus 로고
    • Purification and characterization of a soluble nucleoside diphosphate kinase in Trypanosoma cruzi
    • Ulloa R.M., Muschietti J.P., Veron M., Torres H.N., and Tellez-Inon M.T. Purification and characterization of a soluble nucleoside diphosphate kinase in Trypanosoma cruzi. Mol. Biochem. Parasitol. 70 (1995) 119-129
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 119-129
    • Ulloa, R.M.1    Muschietti, J.P.2    Veron, M.3    Torres, H.N.4    Tellez-Inon, M.T.5
  • 24
    • 1942502299 scopus 로고    scopus 로고
    • The pentose phosphate pathway in Trypanosoma cruzi
    • Maugeri D.A., and Cazzulo J.J. The pentose phosphate pathway in Trypanosoma cruzi. FEMS Microbiol. Lett. 234 (2004) 117-123
    • (2004) FEMS Microbiol. Lett. , vol.234 , pp. 117-123
    • Maugeri, D.A.1    Cazzulo, J.J.2
  • 25
    • 0016773118 scopus 로고
    • A reactive arginine in adenylate kinase
    • Berghauser J. A reactive arginine in adenylate kinase. Biochim. Biophys. Acta 397 (1975) 370-376
    • (1975) Biochim. Biophys. Acta , vol.397 , pp. 370-376
    • Berghauser, J.1
  • 26
    • 0024674189 scopus 로고
    • On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes
    • Cazzulo J.J., Cazzulo Franke M.C., and Franke de Cazzulo B.M. On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes. FEMS Microbiol. Lett. 50 (1989) 259-263
    • (1989) FEMS Microbiol. Lett. , vol.50 , pp. 259-263
    • Cazzulo, J.J.1    Cazzulo Franke, M.C.2    Franke de Cazzulo, B.M.3
  • 29
    • 0027178341 scopus 로고
    • Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe
    • Konrad M. Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 268 (1993) 11326-11334
    • (1993) J. Biol. Chem. , vol.268 , pp. 11326-11334
    • Konrad, M.1
  • 30
  • 31
    • 0030199163 scopus 로고    scopus 로고
    • Diadenosine 5′,5‴-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)-purification, biochemical properties and behaviour during stress
    • Feussner K., Guranowski A., Kostka S., and Wasternack C. Diadenosine 5′,5‴-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)-purification, biochemical properties and behaviour during stress. Z. Naturforsch., C 51 (1996) 477-486
    • (1996) Z. Naturforsch., C , vol.51 , pp. 477-486
    • Feussner, K.1    Guranowski, A.2    Kostka, S.3    Wasternack, C.4
  • 32
    • 0035854697 scopus 로고    scopus 로고
    • Rapid changes in polyphosphate content within acidocalcisomes in response to cell growth, differentiation, and environmental stress in Trypanosoma cruzi
    • Ruiz F.A., Rodrigues C.O., and Docampo R. Rapid changes in polyphosphate content within acidocalcisomes in response to cell growth, differentiation, and environmental stress in Trypanosoma cruzi. J. Biol. Chem. 276 (2001) 26114-26121
    • (2001) J. Biol. Chem. , vol.276 , pp. 26114-26121
    • Ruiz, F.A.1    Rodrigues, C.O.2    Docampo, R.3
  • 34
    • 2942598070 scopus 로고    scopus 로고
    • Adenylate kinase and GTP:AMP phosphotransferase of the malarial parasite Plasmodium falciparum. Central players in cellular energy metabolism
    • Ulschmid J.K., Rahlfs S., Schirmer R.H., and Becker K. Adenylate kinase and GTP:AMP phosphotransferase of the malarial parasite Plasmodium falciparum. Central players in cellular energy metabolism. Mol. Biochem. Parasitol. 136 (2004) 211-220
    • (2004) Mol. Biochem. Parasitol. , vol.136 , pp. 211-220
    • Ulschmid, J.K.1    Rahlfs, S.2    Schirmer, R.H.3    Becker, K.4
  • 35
    • 0842323771 scopus 로고    scopus 로고
    • Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice
    • Dzeja P.P., Terzic A., and Wieringa B. Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice. Mol. Cell. Biochem. 256-257 (2004) 13-27
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 13-27
    • Dzeja, P.P.1    Terzic, A.2    Wieringa, B.3
  • 36
    • 0038644934 scopus 로고    scopus 로고
    • Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism
    • Janssen E., de Groof A., Wijers M., Fransen J., Dzeja P.P., Terzic A., and Wieringa B. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism. J. Biol. Chem. 278 (2003) 12937-12945
    • (2003) J. Biol. Chem. , vol.278 , pp. 12937-12945
    • Janssen, E.1    de Groof, A.2    Wijers, M.3    Fransen, J.4    Dzeja, P.P.5    Terzic, A.6    Wieringa, B.7
  • 37
    • 0029941281 scopus 로고    scopus 로고
    • Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism
    • Lu Q., and Inouye M. Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 5720-5725
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5720-5725
    • Lu, Q.1    Inouye, M.2


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