β-Galactosidase at the membrane-water interface: A case of an active enzyme with non-native conformation

Colloids and Surfaces B: Biointerfaces

Volumn 108, Issue , 2013, Pages 1-7

  Sánchez, Julieta M ^a   Nolan, Verónica ^a   Perillo, María A ^a  

^a UNIVERSIDAD NACIONAL DE CÓRDOBA   (Argentina)

Author keywords

Galactosidase; CD; DSC; Steady state fluorescence; Structure activity relationship; Thermal unfolding

Indexed keywords

CD; DSC; GALACTOSIDASES; STEADY STATE FLUORESCENCES; STRUCTURE/ACTIVITY RELATIONSHIP; THERMAL UNFOLDING;

CATALYST ACTIVITY; CONFORMATIONS; ESCHERICHIA COLI; FLUORESCENCE; INTERFACE STATES; LIPIDS; POPULATION STATISTICS;

PROTEINS;

ACRYLAMIDE; BETA GALACTOSIDASE; LIPOSOME; PHOSPHATIDYLCHOLINE;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; LIPID BILAYER; MEMBRANE BIOLOGY; MEMBRANE WATER INTERFACE; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; TEMPERATURE DEPENDENCE;

BACTERIAL PROTEINS; BETA-GALACTOSIDASE; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; EGG YOLK; ESCHERICHIA COLI; KINETICS; MEMBRANES, ARTIFICIAL; PHOSPHATIDYLCHOLINES; PROTEIN CONFORMATION; PROTEIN UNFOLDING; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SURFACE PROPERTIES; THERMODYNAMICS; WATER;

ESCHERICHIA COLI;

EID: 84875582931     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2013.02.019     Document Type: Article

References (37)

1. Corsico B., Franchini G.R., Hsu K.-T., Storch J. Fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions. J. Lipid Res. 2005, 46:1765-1772.
2. Nolan V., Perduca M., Monaco H.L., Maggio B., Montich G.G. Interactions of chicken liver basic fatty acid-binding protein with lipid membranes. Biochim. Biophys. Acta 2003, 1611:98-106.
3. Gogvadze V., Orrenius S., Zhivotovsky B. Multiple pathways of cytochrome c release from mitochondria in apoptosis. Biochim. Biophys. Acta (BBA) - Bioenerg. 2006, 1757:639-647.
4. Johnson J.E., Cornell R.B. Amphitropic proteins: regulation by reversible membrane interactions (review). Mol. Membr. Biol. 1999, 16:217-235.
5. Roth M.G. Clathrin-mediated endocytosis before fluorescent proteins. Nat. Rev. Mol. Cell Biol. 2006, 7:63-68.
6. Angeletti S., Sanchez J.M., Genti Raimondi S., Perillo M.A. StarD7 behaves as a fusogenic protein in model and cell membrane bilayers. BBA - Biomembranes 2011, 1818:425-433.
7. Walter N. The mystery of nonclassical protein secretion. Eur. J. Biochem. 2003, 270:2109-2119.
8. Booth P.J., Curran A.R. Membrane protein folding. Curr. Opin. Struct. Biol. 1999, 9:115-121.
9. Taniguchi H. Protein myristoylation in protein-lipid and protein-protein interactions. Biophys. Chem. 1999, 82:129-137.
10. Davies S.M.A., Epand R.M., Kraayenhof R., Cornell R.B. Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy. Biochemistry 2001, 40:10522-10531.
11. Sanchez J.M., Perillo M.A. [alpha]-Amylase kinetic parameters modulation by lecithin vesicles: binding versus entrapment. Colloids Surf., B 2000, 18:31-40.
12. Sanchez J.M., Perillo M.A. Membrane adsorption or penetration differentially modulates beta-galactosidase activity against soluble substrates. Colloids Surf., B 2002, 24:21-31.
13. Martini M.F., Disalvo E.A. Superficially active water in lipid membranes and its influence on the interaction of an aqueous soluble protease. Biochim. et Biophys. Acta (BBA) - Biomembrane. 2007, 1768:2541-2548.
14. Sanchez J.M., Perillo M.A. Membrane topology modulates beta-galactosidase activity against soluble substrates. Biophys. Chem. 2002, 99:281-295.
15. Khmelnitsky Y.L., Gladilin A.K., Roubailo V.L., Martinek K., Levashov A.V. Reversed micelles of polymeric surfactants in nonpolar organic solvents. Eur. J. Biochem. 1992, 206:737-745.
16. Martini M.F., Disalvo E.A. Effect of polar head groups on the activity of aspartyl protease adsorbed to lipid membranes. Chem. Phys. Lipids 2003, 122:177-183.
17. Sanchez J.M., Ciklic I., Perillo M.A. Effect of partitioning equilibria on the activity of beta-galactosidase in heterogeneous media. Biophys. Chem. 2005, 118:69-77.
18. Sanchez J.M., Turina A.V., Perillo M.A. Spectroscopic probing of ortho-nitrophenol localization in phospholipid bilayers. J. Photochem. Photobiol. B 2007, 89:56-62.
19. Clop E.M., Clop P.D., Sanchez J.M., Perillo M.A. Molecular packing tunes the activity of Kluyveromyces lactis beta-galactosidase incorporated in Langmuir-Blodgett films. Langmuir 2008, 24:10950-10960.
20. Bangham D., Hill M.W., Miller N.G.A. Preparation and use of liposomes as models of biological membranes. Methods in Membrane Biology 1974, vol. 1:1-68. Plenum Press, New York.
21. Cevc G., Marsh D. Phospholipid Bilayers. Physical Principles and Models 1987, Wiley Interscience, New York.
22. Wallenfels K., Malhota O.P., Galactosidases Adv. Carbohydr. Chem. 1961, 16:239-298.
23. Lakowickz J.R. Topics in Fluorescence Spectroscopy 1991, Plenum Press, New York.
24. Gopalan V., Golbik R., Schreiber G., Fersht A., Altman S. Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli. J. Mol. Biol. 1997, 267:765-769.
25. Landbury J.E., Chowdhry B.Z. Biocalorimetry Applications of Calorimetry in the Biological Sciences 1998, John Wiley and Sons Ltd, West Sussex, England.
26. Lissi E.A., Encinas M.V., Bertolotti S.G., Cosa J.J., Previtali C.M. Fluorescence quenching of indolic compounds in reverse micelles of AOT. Photochem. Photobiol. 1990, 51:53-58.
27. D'Auria S., Cesare N.D., Gryczynski I., Rossi M., Lakowicz J.R. On the Effect of sodium dodecyl sulfate on the structure of {beta}-galactosidase from escherichia coli. a fluorescence study. J. Biochem. 2001, 130:13-18.
28. Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A. Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer. Biochemistry 2003, 42:1796-1803.
29. Burgos I., Dassie S.A., Fidelio G.D. Thermodynamic model for the analysis of calorimetric data of oligomeric proteins. J. Phys. Chem. 2008, 112:14325-14333.
30. Edwards R.A., Jacobson A.L., Huber R.E. Thermal denaturation of .beta.-galactosidase and of two site specific mutants. Biochemistry 1990, 29:11001-11008.
31. Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 1994, 66:482-501.
32. Schymkowitz J.W.H., Rousseau F., Serrano L. Surfing on protein folding energy landscapes. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:15846-15848.
33. Arrondo J.L.R., Muga A., Castresana J., Bernabeu C., Goñi F.M. An infrared spectroscopic study of β-galactosidase structure in aqueous solutions. FEBS Lett. 1989, 252:118-120.
34. Malkov S.N., Zivkovic M.V., Beljanski M.V., Hall M.B., Zaric S.D. A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure. J. Mol. Model 2008, 8:769-775.
35. Jacobson R.H., Zhang X.J., DuBose R.F., Matthews B.W. Three-dimensional structure of [beta]-galactosidase from E. coli. Nature 1994, 369:761-766.
36. Fersht A., Structure Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding 1999, Freeman, New York.
37. Nichtl A., Buchner J., Jaenicke R., Rudilph R., Scheibel T. Folding and association of beta-galactosidase. J. Mol. Biol. 1998, 282:1083-1091.