Evolution of the arginine kinase gene family

Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

Volumn 1, Issue 2, 2006, Pages 209-218

  Uda, Kouji ^a   Fujimoto, Naka ^a   Akiyama, Youhei ^a   Mizuta, Kanae ^a   Tanaka, Kumiko ^a   Ellington, W Ross ^b   Suzuki, Tomohiko ^a  

^a KOCHI UNIVERSITY   (Japan)

^b FLORIDA STATE UNIVERSITY   (United States)

Author keywords

Arginine kinase; Creatine kinase; Exon intron organization; Gene; Phosphagen kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; ARGININE KINASE; CREATINE KINASE; GENOMIC DNA; PHOSPHATE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTHROPOD; ARTICLE; CELLULAR DISTRIBUTION; COELENTERATE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; EXON; EXPRESSED SEQUENCE TAG; GENE DUPLICATION; GENE SEQUENCE; GENE STRUCTURE; GENETIC CONSERVATION; GENETIC VARIABILITY; INTRON; MOLECULAR MECHANICS; MOLLUSC; NEMATODE; NONHUMAN; PHYLOGENY; PLATYHELMINTH; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTOZOON; SCHISTOSOMA; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE;

ARTHROPODA; BIVALVIA; CAENORHABDITIS; CEPHALOPODA; CNIDARIA; COELENTERATA; CRASSOSTREA GIGAS; INVERTEBRATA; MOLLUSCA; NAUTILUS POMPILIUS; NEMATODA; PLATYHELMINTHES; PROTOZOA; SCHISTOSOMA; SCHISTOSOMA MANSONI;

EID: 33646505719     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2005.10.007     Document Type: Article

References (49)

1. Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., and Venter J.C. The genome sequence of Drosophila melanogaster. Science 287 (2000) 2185-2195
2. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: signalP 3.0. J. Mol. Biol. 340 (2004) 783-795
3. Cavalier-Smith T. The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. Int. J. Syst. Evol. Microbiol. 52 (2002) 297-354
4. Chamberlin M. Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta). J. Exp. Biol. 200 (1997) 2789-2796
5. Claros M.G., and Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241 (1996) 770-786
6. Compaan D.M., and Ellington W.R. Functional consequences of a gene duplication and fusion event in an arginine kinase. J. Exp. Biol. 206 (2003) 1545-1556
7. Doumen C., and Ellington W.R. Mitochondrial arginine kinase from the heart of the horseshoe crab, Limulus polyphemus. J. Comp. Physiol., B 160 (1990) 449-457
8. Ellington W.R. Evolution and physiological roles of phosphagen systems. Ann. Rev. Physiol. 63 (2001) 289-325
9. Ellington W.R., and Hines A.C. Mitochondrial activities of phosphagen kinases are not widely distributed in the invertebrates. Biol. Bull. 180 (1991) 505-507
10. Emanuelsson O., Nielsen H., Brunak S., and von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300 (2000) 1005-1016
11. Gattis J.L., Ruben E., Fenley M.O., Ellington W.R., and Chapman M.S. The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants. Biochemistry 43 (2004) 8680-8689
12. Hartl F.U., Pfanner N., Nicholson D.W., and Neupert W. Mitochondrial protein import. Biochim. Biophys. Acta 988 (1989) 1-45
13. Hird F.J.R., and McLean R.M. Synthesis of phosphocreatine and phosphoarginine by mitochondria from various sources. Comp. Biochem. Physiol., B 76 (1983) 41-46
14. Hird F.J.R., and Robin Y. Studies on phosphagen synthesis by mitochondrial preparations. Comp. Biochem. Physiol., B 80 (1985) 517-520
15. Kenyon G.L., and Reed G.H. Creatine kinase: structure-activity relationships. Adv. Enzymol. Relat. Areas Mol. Biol. 54 (1983) 367-426
16. Klein S.C., Haas R.C., Perryman M.B., Billadello J.J., and Strauss A.W. Regulatory element analysis and structural characterization of the human sarcomeric mitochondrial creatine kinase gene. J. Biol. Chem. 266 (1991) 18058-18065
17. Morrison J.F. Arginine kinase and other invertebrate guanidino kinases. In: Boyer P.C. (Ed). The Enzymes (1973), Academic Press, New York 457-486
18. Mühlebach S.M., Gross M., Wirz T., Wallimann T., Perriard J.-C., and Wyss M. Sequence homology and structure predictions of the creatine kinase isoenzymes. Mol. Cell. Biochem. 133-134 (1994) 245-262
19. Mühlebach S.M., Wirz T., Brandle U., and Perriard J.C. Evolution of the creative kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene. J. Biol. Chem. 271 (1996) 11920-11929
20. Munneke L.R., and Collier G.E. Cytoplasmic and mitochondrial arginine kinases in Drosophila: evidence for a single gene. Biochem. Genet. 261 (1988) 131-141
21. Nakai K., and Horton P. PSORT: a program for detecting the sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24 (1999) 34-35
22. Noguchi M., Sawada T., and Akazawa T. ATP-regenerating system in the cilia of Paramecium caudatum. J. Exp. Biol. 204 (2001) 1063-1071
23. Pereira C.A., Alonso G.D., Paveto M.C., Iribarren A., Cabanas M.L., Torres H.N., and Flawia M.M. Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites. J. Biol. Chem. 275 (2000) 1495-1501
24. Pineda Jr. A.O., and Ellington W.R. Immunogold transmission electron microscopic localization of arginine kinase in arthropod mitochondria. J. Exp. Zool. 281 (1998) 73-79
25. Pineda Jr. A.O., and Ellington W.R. Organization of the gene for an invertebrate mitochondrial creatine kinase: comparisons with genes of higher forms and correlation of exon boundaries with functional domains. Gene 265 (2001) 115-121
26. Perovic-Ottstadt S., Wiens M., Schroder H.C., Batel R., Giovine M., Krasko A., Muller I.M., and Muller W.E. Arginine kinase in the demosponge Suberites domuncula: regulation of its expression and catalytic activity by silicic acid. J. Exp. Biol. 208 (2005) 637-646
27. Pruett P.S., Azzi A., Clark S.A., Youseff M.S., Gattis J.L., Somasundaram T., Ellington W.R., and Chapman M.S. The catalytic bases, at most, have an accessory role in the mechanism of arginine kinase. J. Biol. Chem. 278 (2003) 26952-26957
28. Sona S., Suzuki T., and Ellington W.R. Cloning and expression of mitochondrial and protoflagellar creatine kinases from a marine sponge: implications for the origin of intracellular energy transport systems. Biochem. Biophys. Res. Commun. 317 (2004) 1207-1214
29. Stein L.D., Harn D.A., and David J.R. A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure. J. Biol. Chem. 265 (1990) 6582-6588
30. Suzuki T., and Furukohri T. Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237 (1994) 353-357
31. Suzuki T., and Yamamoto Y. Gene structure of two-domain arginine kinases from Anthopleura japonicus and Pseudocardium sachalinensis. Comp. Biochem. Physiol., B 127 (2000) 513-518
32. Suzuki T., Kawasaki Y., Furukohri T., and Ellington W.R. Evolution of phosphagen kinase: VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site. Biochim. Biophys. Acta 1343 (1997) 152-159
33. Suzuki T., Kawasaki Y., and Furukohri T. Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus. Biochem. J. 328 (1997) 301-306
34. Suzuki T., Kawasaki Y., Unemi Y., Nishimura Y., Soga T., Kamidochi K., Yazawa Y., and Furukohri T. Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases-a two-domain arginine kinase from the clam Pseudocardium sachalinensis. Biochim. Biophys. Acta 1388 (1998) 253-259
35. Suzuki T., Kamidochi M., Inoue N., Kawamichi H., Yazawa Y., Furukohri T., and Ellington W.R. Arginine kinase evolved twice: evidence that echinoderm arginine kinase originated from creatine kinase. Biochem. J. 340 (1999) 671-675
36. Suzuki T., Yamamoto Y., and Umekawa M. Stichopus japonicus arginine kinase: gene structure and unique substrate recognition system. Biochem. J. 351 (2000) 579-585
37. Suzuki T., Fukuta H., Nagato H., and Umekawa M. Arginine kinase from Nautilus pompilius, a living fossil. Site-directed mutagenesis studies on the role of amino acid residues in GS (guanidino specificity) region. J. Biol. Chem. 275 (2000) 23884-23890
38. Suzuki T., Sugimura N., Taniguchi T., Unemi Y., Murata T., Hayashida M., Yokouchi K., Uda K., and Furukohri T. Two-domain arginine kinases from the clams Solen strictus and Corbicula japonica. Exceptional amino acid replacement of the functionally important D62 by G. Int. J. Biochem. Cell Biol. 34 (2002) 1221-1229
39. Suzuki T., Mizuta C., Uda K., Ishida K., Mizuta K., Sona S., Compaan D.M., and Ellington W.R. Evolution and divergence of the genes for cytoplasmic, mitochondrial and flagellar creatine kinases. J. Mol. Evol. 59 (2004) 218-226
40. Takeuchi M., Mizuta C., Uda K., Fujimoto N., Okamoto M., and Suzuki T. Unique evolution of bivalvia arginine kinases. Cell. Mol. Life Sci. 61 (2004) 110-117
41. Uda K., Saishoji N., Ichinari S., Ellington W.R., and Suzuki T. Origin and properties of cytoplasmic and mitochondrial isoforms of taurocyamine kinase. FEBS J. 272 (2005) 3521-3530
42. van Thoai N. Homologous phosphagen phosphokinases. In: van Thoai N., and Roche J. (Eds). Homologous Enzymes and Biochemical Evolution (1968), Gordon and Breach, New York 199-229
43. Watts D.C. The origin and evolution of phosphagen phosphotransferases. In: van Thoai N., and Roche J. (Eds). Homologous Enzymes and Biochemical Evolution (1968), Gordon and Breach, New York 279-296
44. Watts D.C. Evolution of phosphagen kinases in the chordate line. Symp. Zool. Soc. Lond. 36 (1975) 105-127
45. Watts D.C., and Bannister L.H. Location of arginine kinase in the cilia of Tetrahymena pyriformis. Nature 226 (1970) 450-451
46. Wothe D.D., Charbonneau H., and Shapiro B.M. The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 5203-5207
47. Wyss M., Smeitink J., Wevers R.A., and Wallimann T. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim. Biophys. Acta 1102 (1992) 119-166
48. Wyss M., Maughan D., and Wallimann T. Re-evaluation of the structure and physiological function of guanidino kinases in fruitfly (Drosophila), sea urchin (Psammechinus miliaris) and man. Biochem. J. 309 (1995) 255-261
49. Zhou G., Somasundaram T., Blanc E., Parthasarathy G., Ellington W.R., and Chapman M.S. Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8449-8454