The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase

BMC Biochemistry

Volumn 7, Issue , 2006, Pages

  Siadat, Omid Ranaei ^a,b   Lougarre, Andrée ^a   Lamouroux, Lucille ^a   Ladurantie, Caroline ^a   Fournier, Didier ^a  

^a INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

^b New Ideas Research Group NIRG   (Iran)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; CYSTEINE DERIVATIVE; ORGANIC SOLVENT; PROTEINASE; UREA;

ARTICLE; DISULFIDE BOND; DROSOPHILA MELANOGASTER; NONHUMAN; PROTEIN DENATURATION; PROTEIN STABILITY;

ACETONITRILES; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; ANIMALS; BACULOVIRIDAE; CYSTINE; DISULFIDES; DNA, COMPLEMENTARY; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; HOT TEMPERATURE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PRONASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SOLVENTS; UREA;

DROSOPHILA MELANOGASTER;

EID: 33745328074     PISSN: 14712091     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-7-12     Document Type: Article

References (46)

1. Marty JL, Sode K, Karube I: Biosensor for detection of organophosphate and carbamate insecticides. Electroanalysis 1992, 4:801-803.
2. Bachmann TT, Leca B, Vilatte F, Marty JL, Fournier D, Schmid RD: Improved multianalyte detection of organophosphates and carbamates with disposable multielectrode biosensors using recombinant mutants of Drosophila acetylcholinesterase and artificial neural networks. Biosens Bioelectron 2000, 15(3-4):193-201.
3. Villatte F, Marcel V, Estrada-Mondaca S, Fournier D: Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides. Biosens Bioelectron 1998, 13(2):157-164.
4. Boublik Y, Saint-Aguet P, Lougarre A, Arnaud M, Villatte F, Estrada-Mondaca S, Fournier D: Acetylcholinesterase engineering for detection of insecticide residues. Protein Eng 2002, 15(1):43-50.
5. Payne CS, Saeed M, Wolfe AD: Ligand stabilization of cholinesterases. Biochim Biophys Acta 1989, 999(1):46-51.
6. Wilson EJ, Massoulie J, Bon S, Rosenberry TL: The rate of thermal inactivation of Torpedo acetylcholinesterase is not reduced in the C231S mutant. FEBS Lett 1996, 379(2):161-164.
7. Estrada-Mondaca S, Fournier D: Stabilization of recombinant Drosophila acetylcholinesterase. Protein Expr Purif 1998, 12(2):166-172.
8. Nasseau M, Boublik Y, Meier W, Winterhalter M, Fournier D: Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation. Biotechnol Bioeng 2001, 75(5):615-618.
9. Fremaux I, Mazeres S, Brisson-Lougarre A, Arnaud M, Ladurantie C, Fournier D: Improvement of Drosophila acetylcholinesterase stability by elimination of a free cysteine. BMC Biochem 2002, 3(1):21.
10. Strub C, Alies C, Lougarre A, Ladurantie C, Czaplicki J, Fournier D: Mutation of exposed hydrophobic amino acids to arginine to increase protein stability. BMC Biochem 2004, 5(1):9.
11. Anfinsen CB, Scheraga HA: Experimental and theoretical aspects of protein folding. Adv Protein Chem 1975, 29:205-300.
12. Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM: Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 2000, 40(1):58-70.
13. Clarke J, Fersht AR: Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 1993, 32(16):4322-4329.
14. Eijsink VG, Bjork A, Gaseidnes S, Sirevag R, Synstad B, van den Burg B, Vriend G: Rational engineering of enzyme stability. J Biotechnol 2004, 113(1-3):105-120.
15. Hall LM, Spierer P: The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader. Embo J 1986, 5(11):2949-2954.
16. Mutero A, Fournier D: Post-translational modifications of Drosophila acetylcholinesterase. In vitro mutagenesis and expression in Xenopus oocytes. J Biol Chem 1992, 267(3):1695-1700.
17. Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL: Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors. Protein Sci 2000, 9(6):1063-1072.
18. [http://bioweb.ensam.inra.fr/ESTHER/general?what=index].
19. [http://www.ncbs.res.in/~faculty/mini/dsdbase/].
20. Dani VS, Ramakrishnan C, Varadarajan R: MODIP revisited: reevaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins. Protein Eng 2003, 16(3):187-193.
21. Ogasahara K, Tsunasawa S, Soda Y, Yutani K, Sugino Y: Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase alpha subunit. Eur J Biochem 1985, 150(1):17-21.
22. Braxton S, Wells JA: Incorporation of a stabilizing Ca(2+)-binding loop into subtilisin BPN′. Biochemistry 1992, 31(34):7796-7801.
23. Villafranca JE, Howell EE, Voet DH, Strobel MS, Ogden RC, Abelson JN, Kraut J: Directed mutagenesis of dihydrofolate reductase. Science 1983, 222(4625):782-788.
24. Perry LJ, Wetzel R: Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation. Science 1984, 226(4674):555-557.
25. Wakarchuk WW, Sung WL, Campbell RL, Cunningham A, Watson DC, Yaguchi M: Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. Protein Eng 1994, 7(11):1379-1386.
26. Villafranca JE, Howell EE, Oatley SJ, Xuong NH, Kraut J: An engineered disulfide bond in dihydrofolate reductase. Biochemistry 1987, 26(8):2182-2189.
27. Matsumura M, Signor G, Matthews BW: Substantial increase of protein stability by multiple disulphide bonds. Nature 1989, 342(6247):291-293.
28. Kanaya S, Katsuda C, Kimura S, Nakai T, Kitakuni E, Nakamura H, Katayanagi K, Morikawa K, Ikehara M: Stabilization of Escherichia coli ribonuclease H by introduction of an artificial disulfide bond. J Biol Chem 1991, 266(10):6038-6044.
29. Mitchinson C, Wells JA: Protein engineering of disulfide bonds in subtilisin BPN′. Biochemistry 1989, 28(11):4807-4815.
30. Eder J, Wilmanns M: Protein engineering of a disulfide bond in a beta/alpha-barrel protein. Biochemistry 1992, 31(18):4437-4444.
31. Mansfeld J, Vriend G, Dijkstra BW, Veltman OR, Van den Burg B, Venema G, Ulbrich-Hofmann R, Eijsink VG: Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J Biol Chem 1997, 272(17):11152-11156.
32. Ivens A, Mayans O, Szadkowski H, Jurgens C, Wilmanns M, Kirschner K: Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge. Eur J Biochem 2002, 269(4):1145-1153.
33. Clarke J, Henrick K, Fersht AR: Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography. J Mol Biol 1995, 253(3):493-504.
34. van den Akker F, Feil IK, Roach C, Platas AA, Merritt EA, Hol WG: Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit. Protein Sci 1997, 6(12):2644-2649.
35. Wells JA, Powers DB: In vivo formation and stability of engineered disulfide bonds in subtilisin. J Biol Chem 1986, 261(14):6564-6570.
36. Betz SF: Disulfide bonds and the stability of globular proteins. Protein Sci 1993, 2(10):1551-1558.
37. Katz BA, Kossiakoff A: The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J Biol Chem 1986, 261(33):15480-15485.
38. Betz SF, Marmorino JL, Saunders AJ, Doyle DF, Young GB, Pielak GJ: Unusual effects of an engineered disulfide on global and local protein stability. Biochemistry 1996, 35(23):7422-7428.
39. Mozhaev VV: Mechanism-based strategies for protein thermostabilization. Trends Biotechnol 1993, 11(3):88-95.
40. Volkin DB, Klibanov AM: Thermal destruction processes in proteins involving cystine residues. J Biol Chem 1987, 262(7):2945-2950.
41. Morel N, Bon S, Greenblatt HM, Van Belle D, Wodak SJ, Sussman JL, Massoulie J, Silman I: Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase. Mol Pharmacol 1999, 55(6):982-992.
42. Ulbrich-Hofmann R, Arnold U, Mansfeld J: The concept of the unfolding region of approaching the mechanism of enzyme stabilization. J Mol Catalysis B: Enzymatic 1999, 7:125-131.
43. Chaabihi H, Fournier D, Fedon Y, Bossy JP, Ravallec M, Devauchelle G, Cerutti M: Biochemical characterization of Drosophila melanogaster acetylcholinesterase expressed by recombinant baculoviruses. Biochem Biophys Res Commun 1994, 203(1):734-742.
44. Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM: A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 1961, 7:88-95.
45. Charpentier A, Menozzi P, Marcel V, Villatte F, Fournier D: A method to estimate acetylcholinesterase-active sites and turnover in insects. Anal Biochem 2000, 285(1):76-81.
46. Betz SF, Pielak GJ: Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry 1992, 31(49):12337-12344.