Structural difference in the H+,K+-ATPase between the E1 and E2 conformations. An attenuated total reflection infrared spectroscopy, UV circular dichroism and raman spectroscopy study

European Journal of Biochemistry

Volumn 262, Issue 1, 1999, Pages 176-183

  Raussens, Vincent ^b   Pezolet M ^b   Ruysschaert, Jean Marie ^b   Goormaghtigh, Erik ^a  

^a FREE UNIVERSITY OF BRUSSELS   (Belgium)

^b NONE

Author keywords

Attenuated total reflection; Fourier transform infrared spectroscopy; Gastric; H+, K+ ATPase; Structural changes

Indexed keywords

HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CIRCULAR DICHROISM; ENZYME CONFORMATION; ENZYME LOCALIZATION; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; RAMAN SPECTROMETRY; STOMACH FUNDUS; SWINE;

ANIMALS; H(+)-K(+)-EXCHANGING ATPASE; PROTEIN CONFORMATION; SPECTRUM ANALYSIS; SWINE;

EID: 0001511119     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00365.x     Document Type: Article

References (51)

1. +)-ATPase. J. Biol. Chem. 261, 16788-16791.
2. +-transporting ATPase. Proc. Natl Acad. Sci. USA 87, 6767-6771.
3. +-adenosinetriphosphatase. Biochemistry 32, 2345-2355.
4. +-ATPase using in vitro translation. J. Biol. Chem. 269, 16909-16919.
5. 5. Sachs, G., Besancon, M., Shin, J.M., Mercier, F., Munson, K. & Hersey, S. (1992) Structural aspects of the gastric H,K-ATPase. J. Bioenerg. Biomembr. 24, 301-308.
6. +-ATPase and of its membrane-associated proteolytic peptides. J. Biol. Chem. 270, 17685-17696.
7. +-ATPase and of its membrane-associated proteolytic peptides. J. Biol. Chem. 272, 262-270.
8. +)-ATPase. Biochim. Biophys. Acta 731, 9-15.
9. +-ATPases. Biochemistry 30, 3503-3510.
10. +)-ATPase studied using tryptic digestion as a tool. Biochim. Biophys. Acta 905, 358-370.
11. 11. Gasset, M., Laynez, J., Menendez, M., Raussens, V. & Goormaghtigh, E. (1997) Structural domain organization of gastric H+,K+-ATPase and its rearrangement during the catalytic cycle. J. Biol. Chem. 272, 1608-1614.
12. 12. Rabon, E.C. & Reuben, M.A. (1990) The mechanism structure gastric H,K-ATpase. Annu. Rev. Physiol. 52, 321-344.
13. 13. Shin, J.M. & Sachs, G. (1994) Identification of a region of the H,K-ATPase alpha subunit associated with the beta subunit. J. Biol. Chem. 269, 8642-8646.
14. +-ATPase alpha subunit is ligand dependent. Proc. Natl Acad. Sci. USA 92, 7936-7940. (Erratum Proc. Natl Acad. Sci. USA 92, 10815)
15. 15. Shainskaya, A. & Karlish, S.J. (1994) Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments. J. Biol. Chem. 269, 10780-10789.
16. +-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach. J. Biol. Chem. 269, 27409-27413.
17. 17. Gresalfi, T.J. & Wallace, B.A. (1984) Secondary structural composition of the Na/K-ATPase E1 and E2 conformers. J. Biol. Chem. 259, 2622-2628.
18. 18. Chetverin, A.B. & Brazhnikov, E.V. (1985) Do sodium and potassium forms of Na,K-ATPase differ in their secondary structure? J. Biol. Chem. 260, 7817-7819.
19. +-ATPase. Biochim. Biophys. Acta 941, 31-38.
20. 20. Soumarmon, A., Abastado, M., Bonfils, S. & Lewin, M.J. (1980) C1-transport in gastric micorsomes. An ATP-dependent influx sensitive to membrane potential and to protein kinase inhibitor. J. Biol. Chem. 255, 11682-11687.
21. 21. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
22. 22. Stanton, M.G. (1968) Colorimetric determination of inorganic phosphate in the presence of biological material and adenosine triphosphate. Anal. Biochem. 22, 27-34.
23. 23. Bensadoun, A. & Weinstein, D. (1976) Assay of proteins in the presence of interfering materials. Anal. Biochem. 70, 241-250.
24. 24. Ljungstrom, M., Norberg, L., Olaisson, H., Wernstedt, C., Vega, F.V., Arvidson, G. & Mardh, S. (1984) Characterization of proton-transporting membranes from resting pig gastric mucosa. Biochim. Biophys. Acta 769, 209-219.
25. 25. Fringeli, U.P. & Gunthard, H.H. (1981) Infrared membrane spectroscopy. Mol. Biol. Biochem. Biophys. 31, 270-332.
26. 26. Kauppinen, J.K., Moffat, D.J. Mantsch, H.H. & Cameron, D.G. (1981) Fourier transform in the computation on self-deconvolution and first-order derivatives spectra of overlapped band contours. Anal. Chem. 53, 1454-1457.
27. 27. Kauppinen, J.K., Moffat, D.J., Mantsch, H.H. & Cameron, D.G. (1981) Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl. Spectrosc. 35, 271-276.
28. 28. Kauppinen, J.K., Moffat, D.J. & Mantsch, H.H. (1981) Noise in Fourier self-deconvolution. Appl. Opt. 20, 1866-1880.
29. 29. Cabiaux, V., Brasseur, R., Wattiez, R., Falmagne, P., Ruysschaert, J.M. & Goormaghtigh, E. (1989) Secondary structure of diphtheria toxin and its fragments interacting with acidic liposomes studied by polarized infrared spectroscopy. J. Biol. Chem. 264, 4928-4938.
30. 30. Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J.M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193, 409-420.
31. 31. Krimm, S. & Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides and proteins. Adv. Prot. Chem. 38, 181-364.
32. 32. Goormaghtigh, E. & Ruysschaert, J.M. (1990) Polarized attenuated total reflection infrared spectroscopy as a tool to investigate the conformation and orientation of membrane components. In Molecular Description of Biological Membrane Components by Computer-Aided Conformational Analysis (Brasseur, R., ed.), pp. 285-329. CRC Press, Boca Raton, FL.
33. 33. Savoie, R., Pézolet, M, Dallaire, S. & Simard, C. (1994) Longitudinal modes in Raman spectra of molecular crystals. Can. J. Appl. Spectrosc. 39, 164-173.
34. 34. de-Jongh, H.H., Goormaghtigh, E. & Killian, J.A. (1994) Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application. Biochemistry 33, 14521-14528.
35. + limb of the pump cycle. J. Biol. Chem. 263, 10705-10710.
36. 36. Goormaghtigh, E., Cabiaux, V. & Ruysschaert. J.M. (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. Subcell. Biochem. 23, 405-450.
37. 37. Tu, A.T. (1982) Raman Spectroscopy in Biology: Principles and Applications. John Wiley & Sons, New York.
38. -1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds. Biochemistry 14, 4870-4876.
39. 39. Yu, N.T. (1974) Comparison of protein structure in crystal, in lyophilized state, and in solution by Raman scattering. III. A-Lactalbumin. J. Am. Chem. Soc. 96, 4664-4667.
40. 40. Spiker R.C., J. & Levin, I.W. (1975) Raman spectra and vibrational assignments for dipalmitoyl phosphatidylcholine and structurally related molecules. Biochim. Biophys. Acta 388, 361-373.
41. +-ATPase studied by attenuated total reflection spectroscopy. Biochim. Biophys. Acta 984, 301-312.
42. 42. Barth, A., Kreutz, W. & Mäntele, W. (1990) Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity. A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle. FEBS Lett. 277, 147-150.
43. 43. Barth, A., Mäntele, W. & Kreutz, W. (1991) Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase. Biochim. Biophys. Acta 1057, 115-123.
44. 2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum. Biochim. Biophys. Acta 1069, 209-217.
45. 45. Raimbault, C., Clottes, E., Leydier, C., Vial, C., & Buchet, R. (1997) ADP-binding and ATP-binding sites in native and proteinase-K-digested creatine kinase, probed by reaction-induced difference infrared spectroscopy. Eur. J. Biochem. 247, 1197-1208.
46. 46. Marrero, H. & Rothschild, K.J. (1987) Conformational changes in bacteriorhodopsin studied by infrared attenuated total reflection. Biophys. J. 52, 629-635.
47. 47. Baenziger, J.E., Miller, K.W. & Rothschild, K.J. (1992) Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy. Biophys. J. 61, 983-992.
48. 48. Baenziger, J.E., Miller, K.W., McCarthy, M.P. & Rothschild, K.J. (1992) Probing conformational changes in the nicotinic acetylcholine receptor by Fourier transform infrared difference spectroscopy. Biophys. J. 62, 64-66.
49. 49. Baenziger, J.E. & Méthot, N. (1995) Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of alpha-helical peptide hydrogens in the nicotinic acetylcholine receptor. J. Biol. Chem. 270, 29129-29137.
50. 50. Méthot, N., McCarthy, M.P. & Baenziger, J.E. (1994) Secondary structure of the nicotinic acetylcholine receptor: implications for structural models of a ligand-gated ion channel. Biochemistry 33, 7709-7717.
51. 51. Méthot, N., Deniers, C.N. & Baenziger, J.E. (1995) Structure of both the ligand- and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange. Biochemistry 34, 15142-15149.