Artículos de revistas
Functional And Small-angle X-ray Scattering Studies Of A New Stationary Phase Survival Protein E (sure) From Xylella Fastidiosa- Evidence Of Allosteric Behaviour
Registro en:
Febs Journal. , v. 276, n. 22, p. 6751 - 6762, 2009.
1742464X
10.1111/j.1742-4658.2009.07390.x
2-s2.0-70350442430
Autor
Saraiva A.M.
Reis M.A.
Tada S.F.
Rosselli-Murai L.K.
Schneider D.R.S.
Pelloso A.C.
Toledo M.A.S.
Giles C.
Aparicio R.
De Souza A.P.
Institución
Resumen
The genome data of bacterium Xylella fastidiosa strain 9a5c has identified several orfs related to its phytopathogenic adaptation and survival. Among these genes, the surE codifies a survival protein E (XfSurE) whose function is not so well understood, but functional assays in Escherichia coli revealed nucleotidase and exopolyphosphate activity. In the present study, we report the XfSurE protein overexpression in E. coli and its purification. The overall secondary structure was analyzed by CD. Small-angle X-ray scattering and gel filtration techniques demonstrated that the oligomeric state of the protein in solution is a tetramer. In addition, functional kinetics experiments were carried out with several monophosphate nucleoside substrates and revealed a highly positive cooperativity. An allosteric mechanism involving torsion movements in solution is proposed to explain the cooperative behaviour of XfSurE. This is the first characterization of a SurE enzyme from a phytopathogen organism and, to our knowledge, the first solution structure of a SurE protein to be described. © 2009 FEBS. 276 22 6751 6762 Dow, J.M., Daniels, M.J., Xylella genomics and bacterial pathogenicity to plants (2000) Yeast, 17, pp. 263-271 Lambais, M.R., Goldman, M.H., Camargo, L.E., Goldman, G.H., A genomic approach to the understanding of Xylella fastidiosa pathogenicity (2000) Curr Opin Microbiol, 3, pp. 459-462 Purcell, A.H., Hopkins, D.L., Fastidious xylem-limited bacterial plant pathogens (1996) Annu Rev Phytopathol, 34, pp. 131-151 Pooler, M.R., Hartung, J.S., Specific PCR detection and identification of Xylella fastidiosa strains causing citrus variegated chlorosis (1995) Curr Microbiol, 31, pp. 377-381 Lee, R.F., Derrick, K.S., Beretta, M.J.G., Chagas, C.M., Rosetti, V., Citros variegated chlorosis: A new destructive disease of citros in Brazil (1991) Citros Ind, 0, pp. 12-15 Simpson, A.J., Reinach, F.C., Arruda, P., Abreu, F.A., Acencio, M., Alvarenga, R., Alves, L.M., Baptista, C.S., The genome sequence of the plant pathogen Xylella fastidiosa. the Xylella fastidiosa consortium of the organization for nucleotide sequencing and analysis (2000) Nature, 406, pp. 151-159 Mura, C., Katz, J.E., Clarke, S.G., Eisenberg, D., Structure and function of an archaeal homolog of survival protein e (SurEalpha): An acid phosphatase with purine nucleotide specificity (2003) J Mol Biol, 326, pp. 1559-1575 Li, C., Ichikawa, J.K., Ravetto, J.J., Kuo, H.C., Fu, J.C., Clarke, S., A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome (1994) J Bacteriol, 176, pp. 6015-6022 Da Silva Neto, J.F., Koide, T., Gomes, S.L., Marques, M.V., The single extracytoplasmic-function sigma factor of Xylella fastidiosa is involved in the heat shock response and presents an unusual regulatory mechanism (2007) J Bacteriol, 189, pp. 551-560 Li, C., Wu, P.Y., Hsieh, M., Growth-phase-dependent transcriptional regulation of the pcm and surE genes required for stationary-phase survival of Escherichia coli (1997) Microbiology, 143, pp. 3513-3520 Visick, J.E., Ichikawa, J.K., Clarke, S., Mutations in the Escherichia coli surE gene increase isoaspartyl accumulation in a strain lacking the pcm repair methyltransferase but suppress stress-survival phenotypes (1998) FEMS Microbiol Lett, 167, pp. 19-25 Riehle, M.M., Bennett, A.F., Long, A.D., Genetic architecture of thermal adaptation in Escherichia coli (2001) Proc Natl Acad Sci USA, 98, pp. 525-530 Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N.N., Kitagawa, M., Mori, H., Savchenko, A., Yakunin, A.F., General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG (2004) J Biol Chem, 279, pp. 54687-54694 Reichard, P., Interactions between deoxyribonucleotide and DNA synthesis (1988) Annu Rev Biochem, 57, pp. 349-374 Galperin, M.Y., Moroz, O.V., Wilson, K.S., Murzin, A.G., House cleaning, a part of good housekeeping (2006) Mol Microbiol, 59, pp. 5-19 Gonçalves, A.M.D., Rêgo, A.T., Thomaz, M., Enguita, F.J., Carrondo, M.A., Expression, purification, crystallization and preliminary X-ray characterization of two crystal forms of stationary-phase survival e protein from Campylobacter jejuni (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, pp. 213-216 Lee, J.Y., Kwak, J.E., Moon, J., Eom, S.H., Liong, E.C., Pedelacq, J.D., Berendzen, J., Suh, S.W., Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family (2001) Nat Struct Biol, 8, pp. 789-794 Zhang, R.G., Skarina, T., Katz, J.E., Beasley, S., Khachatryan, A., Vyas, S., Arrowsmith, C.H., Joachimiak, A., Structure of Thermotoga maritima stationary phase survival protein SurE: A novel acid phosphatase (2001) Structure, 9, pp. 1095-1106 Iwasaki, W., Miki, K., Crystal structure of the stationary phase survival protein SurE with metal ion and AMP (2007) J Mol Biol, 371, pp. 123-136 Pappachan, A., Savithri, H.S., Murthy, M.R.N., Structural and functional studies on a mesophilic stationary phase survival protein (SurE) from Salmonella typhimurium (2008) FEBS J, 275, pp. 5855-5864 Azzoni, A.R., Tada, S.F., Rosselli, L.K., Paula, D.P., Catani, C.F., Sabino, A.A., Barbosa, J.A., Medrano, F.J., Expression and purification of a small heat shock protein from the plant pathogen Xylella fastidiosa (2004) Protein Expr Purif, 33, pp. 297-303 Catani, C.F., Azzoni, A.R., Paula, D.P., Tada, S.F., Rosselli, L.K., De Souza, A.P., Yano, T., Cloning, expression, and purification of the virulence-associated protein D from Xylella fastidiosa (2004) Protein Expr Purif, 37, pp. 320-326 Paula, D.P., Azzoni, A.R., Siqueira, S.F., Catani, C.F., Rosselli, L.K., De Souza, A.P., Expression and purification of a putative H-NS nucleoid-associated protein from the phytopathogen Xylella fastidiosa (2003) Protein Expr Purif, 32, pp. 61-67 Rosselli, L.K., Oliveira, C.L., Azzoni, A.R., Tada, S.F., Catani, C.F., Saraiva, A.M., Soares, J.S., Souza, A.P., A new member of the aldo-keto reductase family from the plant pathogen Xylella fastidiosa (2006) Arch Biochem Biophys, 453, pp. 143-150 Gounaris, K., Selkirk, M.E., Sadeghi, S.J., A nucleotidase with unique atalytic properties is secreted by Trichinella spiralis (2004) Mol Biochem Parasitol, 136, pp. 257-264 Itoh, R., Usami, C., Nishino, T., Tsushima, K., Kinetic properties of cytosol 5′-nucleotidase from chicken liver (1978) Biochim Biophys Acta, 526, pp. 154-162 Bretonnet, A.S., Jordheim, L.P., Dumontet, C., Lancelin, J.M., Regulation and activity of cytosolic 5′-nucleotidase II. A bifunctional allosteric enzyme of the haloacid dehalogenase superfamily involved in cellular metabolism (2005) FEBS Lett, 579, pp. 3363-3368 Spychala, J., Madrid-Marina, V., Fox, I.H., High Km soluble 5′-nucleotidase from human placenta. Properties and allosteric regulation by IMP and ATP (1988) J Biol Chem, 263, pp. 18759-18765 Walldén, K., Stenmark, P., Nyman, T., Flodin, S., Gräslund, S., Loppnau, P., Bianchi, V., Nordlund, P., Crystal structure of human cytosolic 5′-nucleotidase II: Insights into allosteric regulation and substrate recognition (2007) J Biol Chem, 282, pp. 17828-17836 Putnam, C.D., Hammel, M., Hura, G.L., Tainer, J.A., X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution (2007) Q Rev Biophys, 40, pp. 191-285 Svergun, D., Barberato, C., Koch, M.H.J., CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates (1995) J Appl Crystallogr, 28, pp. 768-773 Svergun, D., Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing (1999) Biophys J, 76, pp. 2879-2886 Goodsell, D.S., Olson, A.J., Structural symmetry and protein function (2000) Annu Rev Biophys Biomol Struct, 29, pp. 105-153 Liang, J.Y., Zhang, Y., Huang, S., Lipscomb, W.N., Allosteric transtion of fructose-1,6-bisphosphatase (1993) Proc Natl Acad Sci USA, 90, pp. 2132-2136 Monod, J., Wyman, J., Changeux, J.P., On the nature of allosteric transitions: A plausible model (1965) J Mol Biol, 12, pp. 88-118 Whitmore, L., Wallace, B.A., DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data (2004) Nucleic Acids Res, 32, pp. 668-W673 Whitmore, L., Janes, R.W., Wallace, B.A., Protein Circular Dichroism Data Bank (PCDDB): Data bank and website design (2006) Chirality, 18, pp. 426-429 Whitmore, L., Wallace, B.A., Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases (2008) Biopolymers, 89, pp. 392-400 Geladopoulos, T.P., Sotiroudis, T.G., Evangelopoulos, A.E., A malachite green colorimetric assay for protein phosphatase activity (1991) Anal Biochem, 192, pp. 112-116 Hammersley, A.P., Svensson, S.O., Hanfland, M., Fitch, A.N., Häusermann, D., Two-dimensional detector software: From real detector to idealised image or two-theta scan (1996) High Press Res, 14, pp. 235-248 Glatter, O., Kratky, O., (1982) Small Angle X-ray Scattering., , Academic Press Inc. (London) Ltd. London Svergun, D., Determination of the regularization parameter in indirect-transform methods using perceptual criteria (1992) J Appl Crystallogr, 25, pp. 495-503 Semisotnov, G.V., Kihara, H., Kotova, N.V., Kimura, K., Amemiya, Y., Wakabayashi, K., Serdyuk, I.N., Nikaido, K., Protein globularization during folding. A study by synchrotron small-angle X-ray scattering (1996) J Mol Biol, 262, pp. 559-574 Doniach, S., Changes in biomolecular conformation seen by small angle X-ray scattering (2001) Chem Rev, 101, pp. 1763-1778 Mylonas, E., Svergun, D.I., Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering (2007) J Appl Crystallogr, 40, pp. 245-s249 Volkov, V.V., Svergun, D., Uniqueness of ab initio shape determination in small-angle scattering (2003) J Appl Crystallogr, 36, pp. 860-864 High-throughput structure determination. Proceedings of the 2002 CCP4 (Collaborative Computational Project in Macromolecular Crystallography) Study Weekend. January, 2002. York, United Kingdom (2002) Acta Crystallogr D Biol Crystallogr, 58, pp. 1897-1970. , CCP4 Kozin, M.B., Svergun, D., Automated matching of high- and low-resolution structural models (2001) J Appl Crystallogr, 34, pp. 33-41 Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Lopez, R., ClustalW and ClustalX version 2 (2007) Bioinformatics, 21, pp. 2947-2948 Nicholas, H.B., Nicholas, Jr.K.B., Deerfield, D.W., Genedoc: Analysis and visualization of genetic variation (1997) EMBNEW NEWS, 4, p. 14 McGuffin, L.J., Bryson, K., Jones, D.T., The PSIPRED protein structure prediction server (2000) Bioinformatics, 16, pp. 404-405