New evidence for ATP binding induced catalytic subunit interactions in pig kidney NA/K-ATPase

Journal of Biochemistry

Volumn 140, Issue 4, 2006, Pages 599-607

  Tanoue, Kan ^a   Kaya, Shunji ^a   Hayashi, Yutaro ^b   Abe, Kazuhiro ^a   Imagawa, Toshiaki ^a   Taniguchi, Kazuya ^a   Sakaguchi, Kazuyasu ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b KYORIN UNIVERSITY   (Japan)

Author keywords

Membrane bound enzyme; Na K ATPase; Oligomer; P type ATPase; Subunit interactions

Indexed keywords

4 NITROPHENYLPHOSPHATASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); MAGNESIUM; PHOSPHATASE; PHOSPHOENZYME; SODIUM;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; HYDROLYSIS; KIDNEY; NONHUMAN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; SWINE;

4-NITROPHENYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ANIMALS; CATALYTIC DOMAIN; ENZYME ACTIVATION; KIDNEY; MODELS, BIOLOGICAL; NA(+)-K(+)-EXCHANGING ATPASE; NITROPHENOLS; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHORYLATION; SWINE;

SUS SCROFA;

EID: 33845289734     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj191     Document Type: Article

References (48)

1. 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
2. 2+-ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 73, 269-292
3. Olesen, C., Sørensen, T.L., Nielsen, R.C., Møller, J.V., and Nissen, P. (2004) Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306, 2251-2255
4. Toyoshima, C., Nomura, H., and Tsuda, T. (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368
5. +)ATPase deduced from a complementary DNA. Nature 316, 691-695
6. 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316, 696-700
7. Post, R.L., Hegyvary, C., and Kume, S. (1972) Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540
8. Taniguchi, K. and Post, R.L. (1975) Synthesis of adenosine triphosphate and exchange between inorganic phosphate and adenosine triphosphate in sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 250, 3010-3018
9. Albers, R.W. (1976) The (sodium plus potassium)-transport ATPase in The Enzymes of Biological Membranes (Martonossi, A., ed.) Vol. 3, pp. 283-301, Plenum Publishing Corp., New York
10. +-transporting adenosine triphosphatase in The Enzymes of Biological Membranes (Martonossi, A., ed.) Vol. 3, pp. 35-114, Plenum Publishing Corp., New York
11. Jørgensen, P.L., Hakansson, K.O., and Karlish, S.J. (2003) Structure and mechanism of Na,K-ATPase: functional sites and their interactions. Annu. Rev. Physiol. 65, 817-849
12. 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
13. McIntosh, D.B. (2000) Portrait of a P-type pump. Nat. Struct. Biol. 7, 532-535
14. 2+-ATPase molecules of the sarcoplasmic reticulum. I. Effect of ATP. J. Biol. Chem. 277, 24180-24190
15. +-ATPase: ligand-induced conformational transitions and alterations in subunit interactions evidenced by cross-linking studies. Biochemistry 19, 1132-1140
16. +-ATPase functions in Na/K-ATPase and Related ATPases (Taniguchi, K. and Kaya, S., eds.) pp. 17-26, Elsevier Science, Amsterdam
17. Schoner, W., Thönges, D., Hamer, E., Antolovic, R., Buxbaum, E., Willeke, M., Serpersu, E.H., and Scheiner-Bobis, G. (1994) Is the Sodium pump a functional dimer? in The Sodium Pump. Structure Mechanism, Hormonal Control and its Role in Disease (Bamberg, E. and Schoner, W., eds.) pp. 332-341, Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
18. +-ATPase in Na/K-ATPase and Related ATPases (Taniguchi, K. and Kaya, S., eds.) pp. 349-356, Elsevier Science, Amsterdam
19. i binding to the tetraprotomeric form of Na/K-ATPase accompanying catalytic phosphorylation-dephosphorylation cycle. J. Biol. Chem. 274, 31792-31796
20. Taniguchi, K., Kaya, S., Abe, K., and Mårdh, S. (2001) The oligomeric nature of Na/K-transport ATPase. J. Biochem. 129, 335-342
21. i from one mole of phosphoenzyme formed from a high-affinity ATP binding site and one mole of enzyme-bound ATP at the low-affinity site during cross-talk between catalytic subunits. Biochemistry 41, 2438-2445
22. Abe, K., Kaya, S., Hayashi, Y., Imagawa, T., Kikumoto, M., Oiwa, K., Katoh, T., Yazawa, M., and Taniguchi, K. (2003) Correlation between the activities and the oligomeric forms of pig gastric H/K-ATPase. Biochemistry 42, 15132-15138
23. Abe, K., Kaya, S., Taniguchi, K., Hayashi, Y., Imagawa, T., Kikumoto, M., Oiwa, K., and Sakaguchi, K. (2005) Evidence for a relationship between activity and the tetraprotomeric assembly of solubilized pig gastric H/K-ATPase. J. Biochem. 138, 293-301
24. +-ATPase. Ann. N.Y. Acad. Sci. 986, 232-234
25. +-ATPase by paranitrophenylphosphate (pNPP): evidence for the oligomeric nature of the enzyme. J. Biochem. 116, 1360-1369
26. +-ATPase changes out of phase during sequential appearance of reaction intermediates. J. Biol. Chem. 263, 12943-12947
27. +-ATPase. Biochim. Biophys. Acta 1023, 73-80
28. +)-ATPase. Methods Enzymol. 32, 277-290
29. +-ATPase is the αβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight. Biochim. Biophys. Acta 983, 217-229
30. +)-ATPase determined by low-angle laser light scattering after high-performance gel chromatography. Biochim. Biophys. Acta 748, 153-167
31. Teramachi, S., Imagawa, T., Kaya, S., and Taniguchi, K. (2002) Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase. J. Biol. Chem. 277, 37394-37400
32. +-ATPase: evidence for the binding of ATP to the phosphoenzyme. Biochem. Biophys. Res. Commun. 104, 1447-1453
33. 2+-transport ATPase. J. Biochem. 95, 359-368
34. +-dependent hydrolysis of ATP. J. Biol. Chem. 259, 15228-15233
35. +-ATPase. J. Biol. Chem. 270, 15707-15710
36. +-ATPase. J. Gen. Physiol. 126, 36a
37. +-ATPase, nor Do the sites coexist in native enzyme. J. Biol. Chem. 275, 24512-24517
38. Kanazawa, T., Saito, M., and Tonomura, Y. (1967) Formation and decomposition of a phosphorylated intermediate in the reaction of Na plus-K plus dependent ATPase. J. Biochem. 67, 693-711
39. +-ATPase α-chain with pyridoxal 5′-diphospho-5′-adenosine reduces ATP-dependent phosphorylation stoichiometry from half to a quarter. J. Biol. Chem. 273, 24334-24338
40. +-ATPase. The tetrameric nature of the enzyme. J. Biol. Chem. 273, 24339-24345
41. 2+-ATPase of the sarcoplasmic reticulum. Biochem. J. 356, 685-704
42. Pedemonte, C.H. and Kaplan, J.H. (1990) Chemical modification as an approach to elucidation of sodium pump structure-function relations. Am. J. Physiol. 258, C1-C23
43. Imagawa, T., Kaya, S., and Taniguchi, K. (2003) The amino acid sequence 442GDASE446 in Na/K-ATPase is an important motif in forming the high and low affinity ATP binding pockets. J. Biol. Chem. 278, 50283-50292
44. +-activated adenosinetriphosphatase and itspartial reactions. Biochem. Biophys. Res. Commun. 32, 227-232
45. 32P]phosphoenzyme formed in the presence of potassium ions. Biochim. Biophys. Acta 391, 464-473
46. i, one from one mole of EP and the other from EATP, of oligomeric H/K-ATPase from pig stomach. Ann. N.Y. Acad. Sci. 986, 281-282
47. +-ATPase induced by ATP in The Sodium Pump. Structure, Mechanism, Hormonal Control and its Role in Disease (Bamberg, E. and Schoner, W., eds.) pp. 453-456, Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
48. 2+-ATPase in E1 and E2 states. Biophys. J. 80, 2187-2197