Heterologous expression of 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus: Characterization of the recombinant protein and involvement of disulfide bonds in thermophilicity and thermostability

Protein Expression and Purification

Volumn 16, Issue 1, 1999, Pages 125-135

  Cacciapuoti, Giovanna ^a   Fusco, Stefania ^a   Caiazzo, Natasha ^a   Zappia, Vincenzo ^a   Porcelli, Marina ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; AFFINITY CHROMATOGRAPHY; EXPRESSION VECTOR; PROTEIN EXPRESSION; PROTEIN FOLDING; RECOMBINANT PROTEIN;

ARCHAEA; ESCHERICHIA COLI; SULFOLOBUS SOLFATARICUS;

EID: 0033152019     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1076     Document Type: Article

References (25)

1. Williams-Ashman, H. G., Seidenfeld, J., and Galletti, P. (1982) Trends in the biochemical pharmacology of 5′-deoxy-5′-methylthioadenosine. Biochem. Pharmacol. 31, 277-288.
2. Della Ragione, F., Cartenì-Farina, M., and Zappia, V. (1989) 5′-Deoxy-5′-methylthioadenosine: Novel metabolic and physiological aspects, in "The Physiology of Polyamines" (Bachrach, U., and Heimer, Y. M., Eds.), Vol. 1, pp. 231-251, CRC Press, Boca Raton, FL.
3. Cacciapuoti, G., Porcelli, M., Bertoldo, C., De Rosa, M., and Zappia, V. (1994) Purification and characterization of extremely thermophilic and thermostable 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. J. Biol. Chem. 269, 24762-24769.
4. Cacciapuoti, G., Porcelli, M., Bertoldo, C., Fusco, S., De Rosa, M., and Zappia, V. (1996) Extremely thermophilic and thermostable 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus: Gene cloning and amino acid sequence determination. Eur. J. Biochem. 239, 632-637.
5. Hershfield, M. S., Chafee, S., Koro-Johnson, L., Mary, A., Smith, A., and Short, S. A. (1991) Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl. Acad. Sci. USA 88, 7185-7189.
6. Walton, L., Richards, C. A., and Elwell, L. P. (1989) Nucleotide sequence of the Escherichia coli uridine phosphorylase (udp) gene. Nucleic Acids Res. 17, 6741.
7. Krenitsky, T. A., Koszalka, G. W., and Tuttle, J. V. (1981) Purine nucleoside synthesis, an efficient method employing nucleoside phosphorylases. Biochemistry 20, 3615-3621.
8. Jensen, K. F., and Nygaard, P. (1975) Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium: Purification and some properties. Eur. J. Biochem. 51, 253-256.
9. Cook, W. J., Koszalka, G. W., Hall, W. W., Narayana, S. V. L., and Ealick, S. E. (1987) Crystallization and preliminary X-ray investigation of uridine phosphorylase from Escherichia coli. J. Biol. Chem. 262, 2852-2853.
10. Schlenk, F., and Ehninger, D. J. (1964) Observations on the metabolism of 5′-methylthioadenosine. Arch. Biochem. Biophys. 106, 95-100.
11. Della Ragione, F., Cartenì-Farina, M., Porcelli, M., Cacciapuoti, G., and Zappia, V. (1981) High-performance liquid Chromatographic analysis of 5′-methylthioadenosine in rat tissues. J. Chromatogr. 226, 243-249.
12. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) "Molecular Cloning: A Laboratory Manual," Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
13. Weber, K., Pringle, J. R., and Osborne, M. (1972) Measurement of molecular weight by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 260, 3-27.
14. Della Ragione, F., Porcelli, M., Cartenì-Farina, M., Zappia, V., and Pegg, A. E. (1985) Escherichia coli S-adenosylhomocysteine/5′-methylthioadenosine nucleosidase: Purification, substrate specificity and mechanism of action. Biochem. J. 232, 335-341.
15. Hollecker, M. (1989) Counting integral numbers of residues by chemical modification, in "Protein Structure: A Pratical Approach" (Creighton, T. E., Ed.), pp. 145-153, IRL Press, Oxford.
16. Cacciapuoti, G., Porcelli, M., De Rosa M., Gambacorta, A., Bertoldo, C., and Zappia, V. (1991) S-adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus: Purification, molecular properties and studies on the covalently-bound pyruvate. Eur. J. Biochem. 199, 395-400.
17. Costantino, H. R., Brown, S. H., and Kelly, R. M. (1990) Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115 degrees C. J. Bacteriol. 172, 3654-3660.
18. Cacciapuoti, G., Porcelli, M., Cartenì-Farina, M., Gambacorta, A., and Zappia, V. (1986) Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. Eur. J. Biochem. 161, 263-271.
19. Porcelli, M., Cacciapuoti, G., Cartenì-Farina, M., and Gambacorta, A. (1988) S-adenosylmethionine synthetase in the thermophilic archaebacterium Sulfolobus solfataricus: Purification and characterization of two isoforms. Eur. J. Biochem. 177, 273-280.
20. Ragone, R., Facchiano, F., Cacciapuoti, G., Porcelli, M., and Colonna, G. (1992) Effect of temperature on the propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. 2. Denaturation and structural stability. Eur. J. Biochem. 204, 483-490.
21. Wetzel, R., Perry, L. J., Baase, W. A., and Becktel, W. J. (1988) Disulfide bonds and thermal stability in T4 lysozyme. Proc. Natl. Acad. Sci. USA 85, 401-405.
22. Bardwell, J. C. A. (1994) Building bridges: Disulphide bond formation in the cell. Mol. Microbiol. 14, 199-205.
23. Bardwell, J. C. A., Lee, J.-O., Jander, G., Martin, N., Belin, D., and Beckwith, J. (1993) A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 90, 1038-1042.
24. Wall, G. J., and Pluckthun, A. (1995) Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6, 507-516.
25. Hockney, R. C. (1994) Recent developments in heterologous protein production in Escherichia coli. Trends Biotechnol. 12, 456-463.