Structural characterization of Na,K-ATPase from shark rectal glands by extensive trypsinization

Biochemistry

Volumn 45, Issue 3, 2006, Pages 954-963

  Esmann, Mikael ^a   Arora, Ashish ^b,c   Maunsbach, Arvid B ^a   Marsh, Derek ^b  

^a AARHUS UNIVERSITY   (Denmark)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^c CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CORRELATION METHODS; DIFFUSION; MEMBRANES; PARAMAGNETIC RESONANCE; POLYETHYLENE GLYCOLS; VISCOSITY;

RECTAL GLANDS; TRANSMEMBRANE SEGMENTS; TRYPSINIZATION; TRYPTIC PEPTIDES;

ENZYMES;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); EPITOPE; GLYCEROL; MACROGOL; RUBIDIUM CHLORIDE; SODIUM CHLORIDE; TRYPSIN;

ALPHA CHAIN; ANTIGEN RECOGNITION; AQUEOUS SOLUTION; ARTICLE; BETA CHAIN; CHEMICAL REACTION; COVALENT BOND; DIFFUSION; ELECTRON MICROSCOPY; ELECTRON SPIN RESONANCE; ENZYME STRUCTURE; FREEZE FRACTURE; MASS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; RECTUM GLAND; SEQUENCE ANALYSIS; SHARK; SPIN LABELING; TRYPSINIZATION; VISCOSITY;

AMINO ACID SEQUENCE; ANIMALS; ION CHANNELS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SALT GLAND; SHARKS; TRYPSIN;

CHONDRICHTHYES; SQUALUS ACANTHIAS;

EID: 31044447801     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051573x     Document Type: Article

References (49)

1. Møller, J. V., Juul, B., and le Maire, M. (1996) Structural organization, ion transport, and energy transduction of P-type ATPases, Biochim. Biophys. Acta 1286, 1-51.
2. Kaplan, J. H. (2002) Biochemistry of Na,K-ATPase, Annu. Rev. Biochem. 71, 511-535.
3. Hebert, H., Purhonen, P., Vorum, H., Thomsen, K., and Maunsbach, A. B. (2001) Three-dimensional structure of renal Na,K-ATPase from cryo-electron microscopy of two-dimensional crystals, J. Mol. Biol. 314, 479-494.
4. 2+-ATPase in E1 and E2 states, Biophys. J. 80, 2187-2197.
5. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405, 647-655.
6. Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium, Nature 418, 605-611.
7. Sørensen, T. L.-M., Møller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-1675.
8. Karlish, S. J. D., Goldschleger, R., and Stein, W. D. (1990) A 19-kDa C-terminal tryptic fragment of the α-chain of Na/K-ATPase is essential for occlusion and transport of cations, Proc. Natl. Acad. Sci. U.S.A. 87, 4566-4570.
9. Or, E., Goldshleger, R., Shainskaya, A., and Karlish, S. J. D. (1998) Specific cross-links between fragments of proteolyzed Na,K-ATPase induced by o-phthalaldehyde, Biochemistry 37, 8197-8207.
10. Or, E., Goldshleger, R., and Karlish, S. J. D. (1999) Characterization of disulfide cross-links between fragments of proteolyzed Na,K-ATPase. Implications for spatial organization of transmembrane helices, J. Biol. Chem. 274, 2802-2809.
11. Or, E., Goldshleger, R., Tal, D. M., and Karlish, S. J. D. (1996) Solubilization of a complex of tryptic fragments of Na,K-ATPase containing occluded Rb ions and bound ouabain, Biochemistry 35, 6853-6864.
12. +-ATPase, J. Biol. Chem. 272, 7855-7858.
13. Liu, L., and Askari, A. (1997) Evidence for the existence of two ATP-sensitive Rb+ occlusion pockets within the transmembrane domains of Na+/K+-ATPase, J. Biol. Chem. 272, 14380-14386.
14. 2+)-ATPase from sarcoplasmic reticulum leads to a highly hydrophobic proteinaceous residue with a mainly α-helical structure, Biochemistry 33, 8247-8254.
15. 2+-ATPaSe, a comparison by FTIR after proteolysis treatment of the native membranes, FEBS Lett. 437, 187-192.
16. +-ATPase and of its membrane-embedded region. An attenuated total reflection infrared spectroscopy, circular dichroism and Raman spectroscopy study, Eur. J. Biochem. 252, 261-267.
17. Heimburg, T., Esmann, M., and Marsh, D. (1997) Characterization of the secondary structure and assembly of the transmembrane domains of trypsinized Na,K-ATPase by Fourier transform infrared spectroscopy, J. Biol. Chem. 272, 25685-25692.
18. Esmann, M., Karlish, S. J. D., Sottrup-Jensen, L., and Marsh, D. (1994) Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands, Biochemistry 33, 8044-8050.
19. Esmann, M., Sar, P. C., Hideg, K., and Marsh, D. (1993) Maleimide-, iodoacetamide-, indanedione- and chloromercuric-spin label reagents with derivatized nitroxide rings as ESR reporter groups for protein conformation and dynamics, Anal. Biochem. 213, 336-348.
20. Skou, J. C., and Esmann, M. (1979) Preparation of membrane bound and of solubilized Na,K-ATPase from rectal glands of Squalus acanthias, Biochim. Biophys. Acta 567, 436-444.
21. Esmann, M. (1988) ATPase and phosphatase activity of the Na,K-ATPase; molar and specific activity, protein determinations, Methods Enzymol. 156, 105-115.
22. Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 369-379.
23. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes, J. Biol. Chem. 262, 10035-10038.
24. Ning, G., Maunsbach, A. B., Lee, Y.-J., and Møller, J. V. (1993) Topology of Na,K-ATPase α subunit epitopes analyzed with oligopeptide-specific antibodies and double-labeling immunoelectron microscopy, FEBS Lett. 336, 521-524.
25. 2+ binding properties after removal of cytoplasmic fragments by proteinase K? J. Biol. Chem. 270, 20123-20134.
26. Fajer, P., and Marsh, D. (1982) Microwave and modulation field inhomogeneities and the effect of cavity Q in saturation transfer ESR spectra. Dependence on sample size, J. Magn. Reson. 49, 212-224.
27. Esmann, M., Horváth, L. I., and Marsh, D. (1987) Saturation-transfer electron spin resonance studies on the mobility of spin-labeled sodium and potassium ion activated adenosinetriphosphatase in membranes from Squalus acanthias, Biochemistry 26, 8675-8683.
28. Hemminga, M. A., De Jaeger, P. A., Marsh, D., and Fajer, P. (1984) Standard conditions for the measurement of saturation-transfer ESR spectra, J. Magn. Reson. 59, 160-163.
29. Marsh, D. (1998) Spin label ESR spectroscopy and FTIR spectroscopy for structural/dynamic measurements on ion channels, Methods Enzymol. 294, 59-92.
30. Karlish, S. J. D. (1997) Organization of the membrane domain of the Na/K-pump, Ann. N. Y. Acad. Sci. 834, 30-44.
31. Esmann, M., Christiansen, C., Karlsson, K.-A., Hansson, G. C., and Skou, J. C. (1980) Hydrodynamic properties of solubilized Na,K-ATPase from rectal glands of Squalus acanthias, Biochim. Biophys. Acta 603, 1-12.
32. Ning, G., Esmann, M., and Maunsbach, A. B. (1993) Ultrastructure of membrane-bound Na,K-ATPase after extensive tryptic digestion, FEBS Lett. 330, 19-22.
33. Thomas, D. D., Dalton, L. R., and Hyde, J. S. (1976) Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance, J. Chem. Phys. 65, 3006-3024.
34. Esmann, M., Hideg, K., and Marsh, D. (1994) Influence of poly(ethylene glycol) and aqueous viscosity effects on the rotational diffusion of Na,K-ATPase, Biochemistry 33, 3693-3697.
35. Jørgensen, P. L. (1975) Purification and characterization of Na,K-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool, Biochim. Biophys. Acta 401, 399-415.
36. Cherry, R. J., and Godfrey, R. E. (1981) Anisotropic rotation of bacteriorhodopsin in lipid membranes. Comparison of theory with experiment, Biophys. J. 36, 257-276.
37. Hebert, H., Skriver, E., and Maunsbach, A. B. (1985) Three-dimensional structure of renal Na,K-ATPase determined by electron microscopy of membrane crystals, FEBS Lett. 187, 182-186.
38. Robinson, B. H., and Dalton, L. R. (1980) Anisotropic rotational diffusion studied by passage saturation transfer EPR, J. Chem. Phys. 72, 1312-1324.
39. Marsh, D., and Horváth, L. I. (1989) Spin-label studies of the structure and dynamics of lipids and proteins in membranes, in Advanced EPR. Applications in Biology and Biochemistry (Hoff, A. J., Ed.) pp 707-752, Elsevier, Amsterdam.
40. +-ATPase α subunit is ligand dependent, Proc. Natl. Acad. Sci. U.S.A. 92, 7936-7940.
41. + occlusion and dissociation of the M5/ M6 fragment, J. Biol. Chem. 273, 7311-7319.
42. Donnet, C., Arystarkhova, E., and Sweadner, K. J. (2001) Thermal denaturation of the Na,K-ATPase provides evidence for α-α oligomeric interaction and γ subunit association with the C-terminal domain, J. Biol. Chem. 276, 7357-7365.
43. Arystarkhova, E., Gibbons, D. L., and Sweadner, K. J. (1995) Topology of the Na,K-ATPase, J. Biol. Chem. 270, 8785-8796.
44. Colonna, T. E., Huynh, L., and Fambrough, D. M. (1997) Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system, J. Biol Chem. 272, 12366-12372.
45. Goldshleger, R., Tal, D. M., and Karlish, S. J. D. (1995) Topology of the α-subunit of Na,K-ATPase based on proteolysis. Lability of the topological organization, Biochemistry 34, 8668-8679.
46. Besancon, M., Shin, J. M., Mercier, M., Munson, K., Miller, M., Hersey, S., and Sachs, G. (1993) Membrane topology and omeprazole labeling of the gastric hydrogen ion-potassium-adenosinetriphosphatase, Biochemistry 32, 2345-2355.
47. Shin, J. M., and 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.
48. 2+ binding and energy transduction in Na,K-ATPase, Biochim. Biophys. Acta 1505, 57-74.
49. DeLano, W. L. (2002) The PyMOL Molecular Graphics System on World Wide Web, http://www.pymol.org