Conformational changes and stabilization induced by phosphate binding to 5′-methylthioadenosine phosphorylase from the thermophilic archaeon Sulfolobus solfataricus

Extremophiles

Volumn 5, Issue 5, 2001, Pages 295-302

  Cacciapuoti, Giovanna ^a   Servillo, Luigi ^a   Moretti, Maria Angela ^a   Porcelli, Marina ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

5 Methylthioadenosine phosphorylase; Limited proteolysis; Protein stability; Substrate induced conformational change; Sulfolobus solfataricus

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; 5'-METHYLTHIOADENOSINE PHOSPHORYLASE; DODECYL SULFATE SODIUM; PHOSPHATE; PROTEINASE; PURINE NUCLEOSIDE PHOSPHORYLASE; RECOMBINANT PROTEIN; UREA;

ARTICLE; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION; SPECTROFLUOROMETRY; SULFOLOBUS; TEMPERATURE;

BINDING SITES; ENDOPEPTIDASES; ENZYME STABILITY; PHOSPHATES; PROTEIN CONFORMATION; PURINE-NUCLEOSIDE PHOSPHORYLASE; RECOMBINANT PROTEINS; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; SULFOLOBUS; TEMPERATURE; UREA;

EID: 0035487257     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920100205     Document Type: Article

References (20)

1. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
2. Cacciapuoti G, Porcelli M, Bertoldo C, De Rosa M, 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
3. Cacciapuoti G, Porcelli M, Bertoldo C, Fusco S, De Rosa M, 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
4. Cacciapuoti G, Fusco S, Caiazzo N, Zappia V, Porcelli M (1999) 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 Expr Purif 16:125-135
5. Della Ragione F, Cartenì-Farina M, Zappia V (1989) 5′-Deoxy-5′-methylthioadenosine: novel metabolic and physiological aspects. In: Bachrach U, Heimer YM (eds) The physiology of polyamines, vol 1. CRC Press, Boca Raton, pp 231-251
6. Hershfield MS, Chafee S, Koro-Johnson L, Mary A, Smith A, Short SA (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
7. Jensen KJ (1976) Purine nucleoside phosphorylase from Salmonella typhimurium and Escherichia coli. Initial velocity kinetics, ligand binding and reaction mechanism. Eur J Biochem 61:377-386
8. Jensen KJ, Nygaard P (1975) Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties. Eur J Biochem 51:253-256
9. Kampranis SC, Maxwell A (1998) Conformational changes in DNA girase revealed by limited proteolysis. J Biol Chem 273:22606-22614
10. Kierdaszuk B, Wojcik AM, Shugar D (1997) Binding of phosphate and sulfate anions by purine nucleoside phosphorylase from E. coli: ligand-dependent quenching of enzyme intrinsic fluorescence. Biophys Chem 63:107-118
11. Kline PC, Schramm VL (1993) Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction. Biochemistry 32:13212-13219
12. Koellner G, Luic M, Shugar D, Saenger W, Bzowska A (1998) Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formicin B, a structural analogue of the substrate inosine, and phosphate (sulphate) at 2.1 Å resolution. J Mol Biol 280:153-166
13. Lindsley JE, Wang JC (1993) Study of allosteric communication between promoters by immunotagging. Nature (Lond) 361:749-750
14. Lakowicz JR (1983) In: Principles of fluorescence spectroscopy. Plenum Press, New York, pp 279-284
15. Low LK, Shin HC, Narayan M, Wedemeyer WJ, Scheraga HA (2000) Acceleration of oxidative folding of bovine pancreatic ribonuclease A by anion-induced stabilization and formation of structured native-like intermediates. FEBS Lett 472:67-72
16. Olopade OI, Pomykala HM, Hagos F, Sveen LW, Espinosa R III, Dreyling MH, Gursky S, Stadler WM, Le Beau MM, Bohlander SK (1995) Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21. Proc Natl Acad Sci USA 92:6489-6493
17. Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO (2000) The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J Mol Biol 301:433-450
18. Vogt G, Woell S, Argos P (1997) Protein thermal stability, hydrogen bonds and ion pairs. J Mol Biol 269:631-643
19. Walton L, Richards CA, Elwell LP (1989) Nucleotide sequence of the Escherichia coli uridine phosphorylase (udp) gene. Nucleic Acids Res 17:6741
20. Williams-Ashman HG, Seidenfeld J, Galletti P (1982) Trends in the biochemical pharmacology of 5′-deoxy-5′-methylthioadenosine. Biochem Pharmacol 31:277-288