Characterization of two soluble inorganic pyrophosphatases from Arabidopsis thaliana

Plant Science

Volumn 172, Issue 4, 2007, Pages 796-807

  Navarro De la Sancha, Ernesto ^a   Coello Coutiño, Martha P ^a   Valencia Turcotte, Lilián G ^a   Hernández Domínguez, Eric E ^a   Trejo Yepes, Gisela ^a   Rodríguez Sotres, Rogelio ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

Arabidopsis thaliana; Inorganic pyrophosphatases; Pyrophosphate

Indexed keywords

DNA; HYDROLYSIS; PLANTS (BOTANY); SIZE EXCLUSION CHROMATOGRAPHY;

ARABIDOPSIS THALIANA; INORGANIC PYROPHOSPHATASES; MOLECULAR PROPERTIES; PYROPHOSPHATES;

ENZYME INHIBITION;

CHROMATOGRAPHY; ENZYMES; HYDROLYSIS; NUCLEIC ACIDS; PLANTS;

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 33847317978     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2006.12.011     Document Type: Article

References (40)

1. Sivula T., Salminen A., Parfenyev A.N., Pohjanjoki P., Goldman A., Cooperman B.S., Baykov A.A., and Lahti R. Evolutionary aspects of inorganic pyrophosphatase. FEBS Lett. 454 (1999) 75-80
2. Cooperman B.S., Baykov A.A., and Lahti R. Evolutionary conservation of the active site of soluble inorganic pyrophosphatase. Trends Biochem. Sci. 17 (1992) 262-266
3. Kornberg A. On the metabolic significance of phosphorylic and pyrophosphorylic reactions. In: Kasha M., and Pullman B. (Eds). Horizons in Biochemistry (1962), Academic Press, New York 251-264
4. Lundin M., Baltscheffsky H., and Ronne H. Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function. J. Biol. Chem. 266 (1991) 12168-12172
5. Geigenberger P., Hajirezaei M., Geiger M., Deiting U., Sonnewald U., and Stitt M. Overexpression of pyrophosphatase leads to increased sucrose degradation and starch synthesis, increased activities of enzymes for sucrose-starch interconversions, and increased levels of nucleotides in growing potato tubers. Planta 205 (1998) 428-437
6. Weiner B., Stitt M., and Heldt H.W. Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves. Biochim. Biophys. Acta 893 (1987) 13-21
7. Bucke C. The distribution and properties of alkaline inorganic pyrophosphatase from higher plants. Phytochemistry 9 (1970) 1303-1309
8. Maslowski P., Maslowska H., and Kowalczyk S. Subcellular distribution and properties of alkaline inorganic pyrophosphatase of maize leaves. Acta Biochim. Pol. 24 (1977) 117-126
9. Du Jardin P., Rojas-Beltran J., Gebhardt C., and Brasseur R. Molecular cloning and characterization of a soluble inorganic pyrophosphatase in potato. Plant Physiol. 109 (1995) 853-860
10. Visser K., Heimovaara-Dijkstra S., Kijne J.W., and Wang M. Molecular cloning and characterization of an inorganic pyrophosphatase from barley. Plant Mol. Biol. 37 (1998) 131-140
11. Simmons S., and Butler L.G. Alkaline inorganic pyrophosphatase of maize leaves. Biochim. Biophys. Acta Bioenerg. 172 (1969) 150-157
12. Klemme B., and Jacobi G. Separation and characterization of two inorganic pyrophosphatases from spinach leaves. Planta 120 (1974) 147-153
13. Pwee K.H., and Ho K.K. Identification and characterization of two isoforms of soluble alkaline inorganic pyrophosphatase from sugar cane leaves. Plant Physiol. Biochem. 33 (1995) 39-46
14. Kuhn N.J., and Ward S. Purification, properties, and multiple forms of a manganese-activated inorganic pyrophosphatase from Bacillus subtilis. Arch Biochem. Biophys. 354 (1998) 47-56
15. Heikinheimo P., Tuominen V., Ahonen A.K., Teplyakov A., Cooperman B.S., Baykov A.A., Lahti R., and Goldman A. Toward a quantum-mechanical description of metal-assisted phosphoryl transfer in pyrophosphatase. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 3121-3126
16. Rumsfeld J., Ziegelbauer K., and Spaltmann F. High-throughput assay for inorganic pyrophosphatases using the cytosolic enzymes of Saccharomyces cerevisiae and human as an example. Protein Expr. Purif. 18 (2000) 303-309
17. Cleland W.W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 67 (1963) 104-137
18. Rodriguez-Sotres R., and Muñoz-Clares R.A. Kinetic evidence of the existence of a regulatory phosphoenolpyruvate binding site in maize leaf phosphoenolpyruvate carboxilase. Arch. Biochem. Biophys. 276 (1990) 180-190
19. Schulze S., Mant A., Kossmann J., and Lloyd J.R. Identification of an Arabidopsis inorganic pyrophosphatase capable of being imported into chloroplasts. FEBS Lett. 565 (2004) 101-105
20. Smith K.P., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., and Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150 (1985) 76-85
21. Zor T., and Selinger Z. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 236 (1996) 302-308
22. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
23. 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
24. Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10 (1997) 1-6
25. Andrade M.A., Chacon P., Merelo J.J., and Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
26. Leppanen V.M., Nummelin H., Hansen T., Lahti R., Schafer G., and Goldman A. Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability and effect of metal ion in an archael pyrophosphatase. Protein Sci. 8 (1999) 1218-1231
27. W. Zhou, W. Tempel, Z.J. Liu, L. Chen, L.L. Clancy-Kelley, B.D. Dillard, R.C. Hopkins, W.B. Arendall, J.P. Rose, J.C. Eneh, R.C. Hopkins, F.E. Jenney Jr., H.S. Lee, T. Li, F.L. Poole, C. Shah, F.J. Sugar, M.W.W. Adams, J.S. Richardson, D.C. Richardson, B.C. Wang, Southeast collaboratory for structural genomics inorganic pyrophosphatase from Pyrococcus furiosus PFU-264096-001, pdb entry 1twl.
28. Liu B., Bartlam M., Gao R., Zhou W., Pang H., Liu Y., Feng Y., and Rao Z. Crystal structure of the hyperthermophilic inorganic pyrophosphatase from the archaeon Pyrococcus horikoshii. Biophys. J. 86 (2004) 420-427
29. Kieber J.J., and Signer E.R. Cloning and characterization of an inorganic pyrophosphatase gene from Arabidopsis thaliana. Plant Mol. Biol. 16 (1991) 345-348
30. Teplyakov A., Obmolova G., Wilson K.S., Ishii K., Kaji H., Samejima T., and Kuranova I. Crystal structure of inorganic pyrophosphatase from Thermus thermophilus. Protein Sci. 3 (1994) 1098-1107
31. Kim D.E., Chivian D., and Baker D. Protein structure prediction and analysis using the Roberta server. Nucleic Acids Res. 32 (2004) W526-W531
32. Gómez-García M.R., Losada M., and Serrano A. A novel subfamily of monomeric inorganic pyrophosphatases in photosynthetic eukaryotes. Biochem. J. 395 (2006) 211-221
33. 2+ or CaPPii at atomic resolution and their mechanistic implications. J. Mol. Biol. 314 (2001) 633-645
34. Salvucci M.E., and Crafts-Brandner S.J. Purification and properties of a unique nucleotide pyrophosphatase/phosphodiesterase I that accumulates in soybean leaves in response to fruit removal. Plant Physiol. 108 (1995) 1269-1276
35. Kumar R., and Singh R. Alkaline inorganic pyrophosphatase from immature wheat grains. Phytochemistry 22 (1983) 2405-2407
36. Beitz E. TeXshade: shading and labeling of multiple sequence alignments using LaTeX2e. Bioinformatics 16 (2000) 135-139
37. Volk S.E., Baykov A.A., Duzhenko V.S., and Avaeva S.M. Kinetic studies on the interactions of two forms of inorganic pyrophosphatase of heart mitochondria with physiological ligands. Eur. J. Biochem. 125 (1982) 215-220
38. Lambert S.M., and Watters J.I. The complexes of pyrophosphate ion with alkali metal ions. J. Am. Chem. Soc. 79 (1957) 4262-4265
39. Kotrlý S., and Šůcha L. Handbook of Chemical Equilibria in Analytical Chemistry (1985), Ellis Horwood, London p. 111
40. Zimmermann P., Hirsch-Hoffmann M., Hennig L., and Gruissem W. GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136 (2004) 2621-2632