Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein(372 views) Granata V, Graziano G, Ruggiero A, Raimo G, Masullo M, Arcari P, Vitagliano L, Zagari A
Keywords: Archaea, Circular Dichroism, Elongation Factor, Fluorescence, Protein Stability, Thermal Denaturation, Bacterial Protein, Elongation Factor 1alpha, Article, Controlled Study, Escherichia Coli, Nonhuman, Ph Measurement, Priority Journal, Protein Analysis, Protein Denaturation, Protein Isolation, Sulfolobus Solfataricus, Temperature Sensitivity, Thermostability, Archaeal Proteins, Guanosine Diphosphate, Hydrogen-Ion Concentration, Peptide Elongation Factor 1, Protein Binding, Protein Folding, Protein Structure, Secondary, Tertiary,
Affiliations: *** IBB - CNR ***
Dip. delle Scienze Biologiche, Sez. di Biostrutture, Università degli Studi di Napoli Federico II, Napoli, Italy
CNISM, Università degli Studi di Napoli Federico II, Napoli, Italy
Dip. di Scienze Biologiche ed Ambientali, Università del Sannio, Benevento, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
CIRPEB, Napoli, Italy
Dip. di Scienze e Tecnologie per l'Ambiente e il Territorio, Università degli Studi del Molise, Isernia, Italy
Dip. di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Napoli, Italy
Dip. di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Roccelletta di Borgia, Catanzaro, Italy
CEINGE-Biotecnologie Avanzate, Scarl, Napoli, Italy
CNISM, Universit degli Studi di Napoli Federico II, Napoli, Italy
References: Yonath, A., The search and its outcome: high-resolution structures of ribosomal particles from mesophilic, thermophilic, and halophilic bacteria at various functional states (2002) Annu. Rev. Biophys. Biomol. Struct., 31, pp. 257-27
Nilsson, J., Nissen, P., Elongation factors on the ribosome (2005) Curr. Opin. Struct. Biol., 15, pp. 349-354
Andersen, G.R., Nissen, P., Nyborg, J., Elongation factors in protein biosynthesis (2003) Trends Biochem. Sci., 28, pp. 434-441
Merrick, W.C., Nyborg, J., (2000) Translational Control of Gene Expression, , Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, New York
Gaucher, E.A., Thomson, J.M., Burgan, M.F., Benner, S.A., Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins (2003) Nature, 425, pp. 285-288
Abel, K., Yoder, M.D., Hilgenfeld, R., Jurnak, F., An alpha to beta conformational switch in EF-Tu (1996) Structure, 4, pp. 1153-1159
Berchtold, H., Reshetnikova, L., Reiser, C.O., Schirmer, N.K., Sprinzl, M., Hilgenfeld, R., Crystal structure of active elongation factor Tu reveals major domain rearrangements (1993) Nature, 365, pp. 126-132
Kjeldgaard, M., Nissen, P., Thirup, S., Nyborg, J., The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation (1993) Structure, 1, pp. 35-50
Kjeldgaard, M., Nyborg, J., Refined structure of elongation factor EF-Tu from Escherichia coli (1992) J. Mol. Biol., 223, pp. 721-742
Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B.F., Nyborg, J., Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog (1995) Science, 270, pp. 1464-1472
Vogeley, L., Palm, G.J., Mesters, J.R., Hilgenfeld, R., Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox (2001) J. Biol. Chem., 276, pp. 17149-17155
Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S., Leberman, R., The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution (1996) Nature, 379, pp. 511-518
Wang, Y., Jiang, Y., Meyering-Voss, M., Sprinzl, M., Sigler, P.B., Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus (1997) Nat. Struct. Biol., 4, pp. 650-656
Andersen, G.R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T.G., Kjeldgaard, M., Nyborg, J., Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha (2000) Mol. Cell, 6, pp. 1261-1266
Andersen, G.R., Valente, L., Pedersen, L., Kinzy, T.G., Nyborg, J., Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex (2001) Nat. Struct. Biol., 8, pp. 531-534
Vitagliano, L., Masullo, M., Sica, F., Zagari, A., Bocchini, V., The crystal structure of Sulfolobus solfataricus elongation factor 1a in complex with GDP reveals novel features in nucleotide binding and exchange (2001) EMBO J., 20, pp. 5305-5311
Granata, V., Graziano, G., Ruggiero, A., Raimo, G., Masullo, M., Arcari, P., Vitagliano, L., Zagari, A., Chemical denaturation of the elongation factor 1alpha isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (2006) Biochemistry, 45, pp. 719-726
Vitagliano, L., Ruggiero, A., Masullo, M., Cantiello, P., Arcari, P., Zagari, A., The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with magnesium and GDP (2004) Biochemistry, 43, pp. 6630-6636
Ianniciello, G., Masullo, M., Gallo, M., Arcari, P., Bocchini, V., Expression in Escherichia coli of thermostable elongation factor 1 alpha from the archaeon Sulfolobus solfataricus (1996) Biotechnol. Appl. Biochem., 23, pp. 41-45
Gill, S.C., von Hippel, P.H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
Masullo, M., De Vendittis, E., Bocchini, V., Archaebacterial elongation factor 1 alpha carries the catalytic site for GTP hydrolysis (1994) J. Biol. Chem., 269, pp. 20376-20379
Cantor, C.R., Schimmel, P.R., (1980) Biophysical Chemistry, , W.H. Freeman & Company, New York
Fukada, H., Takahashi, K., Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride (1998) Proteins, 33, pp. 159-166
Sanderova, H., Hulkova, M., Malon, P., Kepkova, M., Jonak, J., Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms (2004) Protein Sci., 13, pp. 89-99
Sedlak, E., Sprinzl, M., Grillenbeck, N., Antalik, M., Microcalorimetric study of elongation factor Tu from Thermus thermophilus in nucleotide-free, GDP and GTP forms and in the presence of elongation factor Ts (2002) Biochim. Biophys. Acta, 1596, pp. 357-365
Zale, S.E., Klibanov, A.M., Why does ribonuclease irreversibly inactivate at high temperatures? (1986) Biochemistry, 25, pp. 5432-5444
Ross, P.D., Shrake, A., Decrease in stability of human albumin with increase in protein concentration (1988) J. Biol. Chem., 263, pp. 11196-11202
Zoldak, G., Sedlak, E., Valusova, E., Wolfrum, A., Marek, J., Antalik, M., Sprinzl, M., Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus effect of the residual structure and intermonomer disulfide bond (2006) Biochim. Biophys. Acta, 1764, pp. 1277-1285
Lakowicz, J.R., (1999) Principles of Fluorescence Spectroscopy, , Kluwer Academic and Plenum Publishers, New York
Chiaraluce, R., Van Der Oost, J., Lebbink, J.H., Kaper, T., Consalvi, V., Persistence of tertiary structure in 7.9 M guanidinium chloride: the case of endo-beta-1,3-glucanase from Pyrococcus furiosus (2002) Biochemistry, 41, pp. 14624-14632
Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., Gilmanshin, R.I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Ptitsyn, O.B., Molten globule and protein folding (1995) Adv. Protein Chem., 47, pp. 83-229
Masullo, M., Raimo, G., Bocchini, V., Resistance of archaebacterial aEF-1 alpha.GDP against denaturation by heat and urea (1993) Biochim. Biophys. Acta, 1162, pp. 35-39
Pyrpassopoulos, S., Ladopoulou, A., Vlassi, M., Papanikolau, Y., Vorgias, C.E., Yannoukakos, D., Nounesis, G., Thermal denaturation of the BRCT tandem repeat region of human tumour suppressor gene product BRCA1 (2005) Biophys. Chem., 114, pp. 1-12
Robic, S., Guzman-Casado, M., Sanchez-Ruiz, J.M., Marqusee, S., Role of residual structure in the unfolded state of a thermophilic protein (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 11345-11349
Melchionna, S., Sinibaldi, R., Briganti, G., Explanation of the stability of thermophilic proteins based on unique micromorphology (2006) Biophys. J., 90, pp. 4204-4212
Del Vecchio, P., Graziano, G., Granata, V., Barone, G., Mandrich, L., Manco, G., Rossi, M., Temperature- and denaturant-induced unfolding of two thermophilic esterases (2002) Biochemistry, 41, pp. 1364-1371
Arcari, P., Masullo, M., Arcucci, A., Ianniciello, G., de Paola, B., Bocchini, V., A chimeric elongation factor containing the putative guanine nucleotide binding domain of archaeal EF-1 alpha and the M and C domains of eubacterial EF-Tu (1999) Biochemistry, 38, pp. 12288-12295
Zagari, A., Sica, F., Scarano, G., Vitagliano, L., Bocchini, V., Crystallization of a hyperthermophilic archaeal elongation factor 1a (1994) J. Mol. Biol., 242, pp. 175-177
Gavin, A.C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Superti-Furga, G., Proteome survey reveals modularity of the yeast cell machinery (2006) Nature, 440, pp. 631-636
Nandan, D., Lopez, M., Ban, F., Huang, M., Li, Y., Reiner, N.E., Cherkasov, A., Indel-based targeting of essential proteins in human pathogens that have close host orthologue(s): discovery of selective inhibitors for Leishmania donovani elongation factor-1alpha (2007) Proteins, 67, pp. 53-64
Haynes, C., Oldfield, C.J., Ji, F., Klitgord, N., Cusick, M.E., Radivojac, P., Uversky, V.N., Iakoucheva, L.M., Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes (2006) PLoS Comput. Biol., 2, pp. e100
Andersen, G. R., Nissen, P., Nyborg, J., Elongation factors in protein biosynthesis (2003) Trends Biochem. Sci., 28, pp. 434-441
Merrick, W. C., Nyborg, J., (2000) Translational Control of Gene Expression, , Sonenberg N., Hershey J. W. B., and Mathews M. B. (Eds), Cold Spring Harbor Laboratory Press, New York
Gaucher, E. A., Thomson, J. M., Burgan, M. F., Benner, S. A., Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins (2003) Nature, 425, pp. 285-288
Andersen, G. R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T. G., Kjeldgaard, M., Nyborg, J., Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A: eEF1Balpha (2000) Mol. Cell, 6, pp. 1261-1266
Andersen, G. R., Valente, L., Pedersen, L., Kinzy, T. G., Nyborg, J., Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex (2001) Nat. Struct. Biol., 8, pp. 531-534
Budkevich, T. V., Timchenko, A. A., Tiktopulo, E. I., Negrutskii, B. S., Shalak, V. F., Petrushenko, Z. M., Aksenov, V. L., El'skaya, A. V., Extended conformation of mammalian translation elongation factor 1A in solution (2002) Biochemistry, 41, pp. 15342-15349
Gill, S. C., von Hippel, P. H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
Cantor, C. R., Schimmel, P. R., (1980) Biophysical Chemistry, , W. H. Freeman & Company, New York
Zale, S. E., Klibanov, A. M., Why does ribonuclease irreversibly inactivate at high temperatures? (1986) Biochemistry, 25, pp. 5432-5444
Ross, P. D., Shrake, A., Decrease in stability of human albumin with increase in protein concentration (1988) J. Biol. Chem., 263, pp. 11196-11202
Lakowicz, J. R., (1999) Principles of Fluorescence Spectroscopy, , Kluwer Academic and Plenum Publishers, New York
Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., Gilmanshin, R. I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Ptitsyn, O. B., Molten globule and protein folding (1995) Adv. Protein Chem., 47, pp. 83-229
Gavin, A. C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Superti-Furga, G., Proteome survey reveals modularity of the yeast cell machinery (2006) Nature, 440, pp. 631-636
Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein
The elongation factors (EF-Tu/EF-1 alpha) are universal proteins, involved in protein biosynthesis. A detailed characterization of the stability against temperature of SsEF-1 alpha, a three-domain protein isolated from the hyperthermophilic archaeon Sulfolobus solfataricus is presented. Thermal denaturation of both the GDP-bound (SsEF-1 alpha center dot GDP) and the ligand-free (nfSsEF-1 alpha) forms was investigated by means of circular dichroism and fluorescence measurements, over the 4. 0-7. 5 pH interval. Data indicate that the unfolding process is cooperative with no intermediate species and that the few inter-domain contacts identified in the crystal structure of SsEF-1 alpha play a role also at high temperatures. Finally, it is shown that the enzyme exhibits two different interchangeable thermally denatured states, depending on pH. (0 2008 Elsevier B. V All rights reserved
Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(449 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote