Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: Over-expression, purification and biophysical characterization

Protein Expression and Purification

Volumn 63, Issue 2, 2009, Pages 147-157

  Zeev Ben Mordehai, Tzviya ^a   Paz, Aviv ^a   Peleg, Yoav ^a   Toker, Lilly ^a   Wolf, Sharon G ^a   Rydberg, Edwin H ^b   Sussman, Joel L ^a   Silman, Israel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b IRBM   (Italy)

Author keywords

Detergent; Expression; Immunoglobulin; Multimers; Pichia; Secretion

Indexed keywords

AMALGAM PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; FRACTALKINE; IMMUNOGLOBULIN; NERVE CELL ADHESION MOLECULE;

AFFINITY CHROMATOGRAPHY; ANIMAL; ARTICLE; BIOSYNTHESIS; CHEMISTRY; DROSOPHILA MELANOGASTER; DRUG EFFECT; GEL CHROMATOGRAPHY; GENE EXPRESSION; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MOLECULAR CLONING; NERVE FIBER; PHYSIOLOGY; PICHIA; TRANSMISSION ELECTRON MICROSCOPY;

ANIMALS; AXONS; CELL ADHESION MOLECULES, NEURONAL; CHEMOKINE CX3CL1; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; GENE EXPRESSION; IMMUNOGLOBULINS; MICROSCOPY, ELECTRON, TRANSMISSION; PICHIA;

PICHIA; PICHIA PASTORIS; TORPEDO CALIFORNICA;

EID: 56349120671     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.09.019     Document Type: Article

References (36)

1. Apic G., Gough J., and Teichmann S.A. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 310 (2001) 311-325
2. Wright C.F., Teichmann S.A., Clarke J., and Dobson C.M. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438 (2005) 878-881
3. Smialowski P., Martin-Galiano A.J., Mikolajka A., Girschick T., Holak T.A., and Frishman D. Protein solubility: sequence based prediction and experimental verification. Bioinformatics 23 (2007) 2536-2542
4. Seeger M.A., Haffley L., and Kaufman T.C. Characterization of amalgam: a member of the immunoglobulin superfamily from Drosophila. Cell 55 (1988) 589-600
5. Williams A.F., and Barclay A.N. The immunoglobulin superfamily-domains for cell surface recognition. Ann. Rev. Immunol. 6 (1988) 381-405
6. Souillac P.O., Uversky V.N., Millett I.S., Khurana R., Doniach S., and Fink A.L. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J. Biol. Chem. 277 (2002) 12657-12665
7. Frémion F., Darboux I., Diano M., Hipeau-Jacquotte R., Seeger M.A., and Piovant M. Amalgam is a ligand for the transmembrane receptor neurotactin and is required for neurotactin-mediated cell adhesion and axon fasciculation in Drosophila. EMBO J. 19 (2000) 4463-4472
8. de la Escalera S., Bockamp E.O., Moya F., Piovant M., and Jimenez F. Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases. EMBO J. 9 (1990) 3593-3601
9. Barthalay Y., Hipeau-Jacquotte R., de la Escalera S., Jimenez F., and Piovant M. Drosophila neurotactin mediates heterophilic cell adhesion. EMBO J. 9 (1990) 3603-3609
10. Zeev-Ben-Mordehai T., Rydberg E.H., Solomon A., Toker L., Auld V.J., Silman I., Botti S., and Sussman J.L. The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. Proteins 53 (2003) 758-767
11. Liebl E.C., Rowe R.G., Forsthoefel D.J., Stammler A.L., Schmidt E.R., Turski M., and Seeger M.A. Interactions between the secreted protein Amalgam, its transmembrane receptor Neurotactin and the Abelson tyrosine kinase affect axon pathfinding. Development 130 (2003) 3217-3226
12. Sussman J.L., Harel M., Frolow F., Varon L., Toker L., Futerman A.H., and Silman I. Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C. J. Mol. Biol. 203 (1988) 821-823
13. Cabrita L.D., Gilis D., Robertson A.L., Dehouck Y., Rooman M., and Bottomley S.P. Enhancing the stability and solubility of TEV protease using in silico design. Protein Sci. 16 (2007) 2360-2367
14. Clare J.J., Romanos M.A., Rayment F.B., Rowedder J.E., Smith M.A., Payne M.M., Sreekrishna K., and Henwood C.A. Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies. Gene 105 (1991) 205-212
15. Grueninger-Leitch F., D'Arcy A., D'Arcy B., and Chene C. Deglycosylation of proteins for crystallization using recombinant fusion protein glycosidases. Protein Sci. 5 (1996) 2617-2622
16. Schuck P., and Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54 (2000) 328-341
17. Laue T.M., Shah B.D., Ridgeway T.M., and Pelletier S.L. Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), The Royal Society of Chemistry, Cambridge
18. Sreekrishna K., Brankamp R.G., Kropp K.E., Blankenship D.T., Tsay J.T., Smith P.L., Wierschke J.D., Subramaniam A., and Birkenberger L.A. Strategies for optimal synthesis and secretion of heterologous proteins in the methylotrophic yeast Pichia pastoris. Gene 190 (1997) 55-62
19. Hao Y., Chu J., Wang Y., Zhuang Y., and Zhang S. The inhibition of aggregation of recombinant human consensus interferon-alpha mutant during Pichia pastoris fermentation. Appl. Microbiol. Biotechnol. 74 (2007) 578-584
20. Woo J.H., Liu Y.Y., and Neville Jr. D.M. Minimization of aggregation of secreted bivalent anti-human T cell immunotoxin in Pichia pastoris bioreactor culture by optimizing culture conditions for protein secretion. J. Biotechnol. 121 (2006) 75-85
21. Cregg J.M., Cereghino J.L., Shi J., and Higgins D.R. Recombinant protein expression in Pichia pastoris. Molec. Biotech. 16 (2000) 23-52
22. Bretthauer R.K., and Castellino F.J. Glycosylation of Pichia pastoris-derived proteins. Biotechnol. Appl. Biochem. 30 Pt 3 (1999) 193-200
23. Darboux I., Barthalay Y., Piovant M., and Hipeau-Jacquotte R. The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties. EMBO J. 15 (1996) 4835-4843
24. Bayley P.M. Circular dichroism and optical rotation. In: Brown S.B. (Ed). An Introduction to Spectroscopy for Biochemists (1980), Academic Press, London 148-235
25. Pioletti M., Findeisen F., Hura G.L., and Minor Jr. D.L. Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer. Nat. Struct. Mol. Biol. 13 (2006) 987-995
26. Tidow H., Melero R., Mylonas E., Freund S.M., Grossmann J.G., Carazo J.M., Svergun D.I., Valle M., and Fersht A.R. Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex. Proc. Natl. Acad. Sci. USA 104 (2007) 12324-12329
27. Souillac P.O., Uversky V.N., Millett I.S., Khurana R., Doniach S., and Fink A.L. Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. J. Biol. Chem. 277 (2002) 12666-12679
28. Litman G.W., Good R.A., Frommel D., and Rosenberg A. Conformational significance of the intrachain disulfide linkages in immunoglobulins. Proc. Natl. Acad. Sci. USA 67 (1970) 1085-1092
29. Shapiro L., Love J., and Colman D.R. Adhesion molecules in the nervous system: structural insights into function and diversity. Annu. Rev. Neurosci. 30 (2007) 451-474
30. Schurmann G., Haspel J., Grumet M., and Erickson H.P. Cell adhesion molecule L1 in folded (horseshoe) and extended conformations. Mol. Biol. Cell. 12 (2001) 1765-1773
31. Freigang J., Proba K., Leder L., Diederichs K., Sonderegger P., and Welte W. The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion. Cell 101 (2000) 425-433
32. Su X.D., Gastinel L.N., Vaughn D.E., Faye I., Poon P., and Bjorkman P.J. Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion. Science 281 (1998) 991-995
33. Schlunegger M.P., Bennett M.J., and Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50 (1997) 61-122
34. Chen C.P., Posy S., Ben-Shaul A., Shapiro L., and Honig B.H. Specificity of cell-cell adhesion by classical cadherins: critical role for low-affinity dimerization through beta-strand swapping. Proc. Natl. Acad. Sci. USA 102 (2005) 8531-8536
35. Raag R., and Whitlow M. Single-chain Fvs. FASEB J. 9 (1995) 73-80
36. Kortt A.A., Malby R.L., Caldwell J.B., Gruen L.C., Ivancic N., Lawrence M.C., Howlett G.J., Webster R.G., Hudson P.J., and Colman P.M. Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur. J. Biochem. 221 (1994) 151-157