Lys691 and Asp714 of the Na+/K +-ATPase α Subunit Are Essential for Phosphorylation, Dephosphorylation, and Enzyme Turnover

Biochemistry

Volumn 43, Issue 16, 2004, Pages 4731-4740

  Su, Ping ^a,b   Scheiner Bobis, Georgios ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; DEHALOGENATION; ESTERIFICATION; HYDROGEN INORGANIC COMPOUNDS; HYDROLYSIS; MUTAGENESIS; PHOSPHATES; PHOSPHORESCENCE; YEAST;

HYDROLASES; PHOSPHORYLATION; SODIUM PUMP SPECIFIC INHIBITOR; SUPERFAMILY;

ENZYMES;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM) INHIBITOR; ASPARTIC ACID; LYSINE; MAGNESIUM ION; OUABAIN; PROTEIN SUBUNIT; ACRYLAMIDE DERIVATIVE; ION CHANNEL; PALYTOXIN; PHOSPHATASE; TRITIUM;

ALPHA CHAIN; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME METABOLISM; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; NONHUMAN; POTASSIUM CELL LEVEL; POTASSIUM TRANSPORT; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; PROTEIN FAMILY; SODIUM CELL LEVEL; SODIUM TRANSPORT; YEAST CELL; ANIMAL; BINDING COMPETITION; CHEMISTRY; DOG; DRUG ANTAGONISM; ENZYMOLOGY; GENE VECTOR; GENETICS; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; SHEEP; SITE DIRECTED MUTAGENESIS;

STROPHANTHUS GRATUS;

ACRYLAMIDES; ANIMALS; ASPARTIC ACID; BINDING, COMPETITIVE; CATALYSIS; DOGS; GENETIC VECTORS; ION CHANNELS; LYSINE; MUTAGENESIS, SITE-DIRECTED; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SHEEP; TRITIUM;

EID: 1942534619     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049884f     Document Type: Article

References (46)

1. Lutsenko, S., and Kaplan, J. H. (1995) Organization of P-type ATPases: significance of structural diversity. Biochemistry 34, 15607-15613.
2. Axelsen, K. B., and Palmgren, M. G. (1998) Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101.
3. Green, N. M. (1992) Ion-Motive ATPases: Structure, Function, and Regulation. Proceedings of a Conference. Cleveland, Ohio, June 13-17, 1992. Ann. N. Y. Acad. Sci. 671, 1-515.
4. Skou, J. C. (1988) The Na, K-pump. Methods Enzymol. 156, 1-25.
5. 2 conformational transitions in Na, K-pump and Ca-pump proteins. J. Membr. Biol. 103, 95-120.
6. Lutsenko, S., and Kaplan, J. H. (1996) P-type ATPases. Trends Biochem. Sci. 21, 467.
7. MacLennan, D. H., and Green, N. M. (2000) Structural biology. Pumping ions. Nature 405, 633-634.
8. Aravind, L., Galperin, M. Y., and Koonin, E. V. (1998) The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23, 127-129.
9. Wang, W., Kim, R., Jancarik, J., Yokota, H., and Kim, S. (2001) Crystal Structure of Phosphoserine Phosphatase from Methanococcus jannaschii, a Hyperthermophile, at 1.8, Å Resolution. Structure 9, 65-72.
10. Kurihara, T., Liu, J. Q., Nardi-Dei, V., Koshikawa, H., Esaki, N., and Soda, K. (1995) Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues. J. Biochem. (Tokyo) 117, 1317-1322.
11. Motosugi, K., and Soda, K. (1984) [Enzymological aspects of halo acid dehalogenation]. Tanpakushitsu Kakusan Koso 29, 101-110.
12. 18O incorporation experiments. J. Biol. Chem. 270, 18309-18312.
13. Ichiyama, S., Kurihara, T., Li, Y. F., Kogure, Y., Tsunasawa, S., and Esaki, N. (2000) Novel catalytic mechanism of nucleophilic substitution by asparagine residue involving cyanoalanine intermediate revealed by mass spectrometric monitoring of an enzyme reaction. J. Biol. Chem. 275, 40804-40809.
14. Hisano, T., Hata, Y., Fujii, T., Liu, J. Q., Kurihara, T., Esaki, N., and Soda, K. (1996) Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold. J. Biol. Chem. 271, 20322-20330.
15. 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.
16. Li, Y. F., Hata, Y., Fujii, T., Hisano, T., Nishihara, M., Kurihara, T., and Esaki, N. (1998) Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism. J. Biol. Chem. 273, 15035-15044.
17. 2+ binding, phosphorylation, and energy transduction in Na, K.-ATPase. J. Biol. Chem. 275, 37588-37595.
18. 2+ binding, phosphorylation, and energy transfer in Na, K.-ATPase. J. Bioenerg. Biomembr. 33, 367-377.
19. Horowitz, B., Eakle, K. A., Scheiner-Bobis, G., Randolph, G. R., Chen, C. Y., Hitzeman, R. A., and Farley, R. A. (1990) Synthesis and assembly of functional mammalian Na, K.-ATPase in yeast. J. Biol. Chem. 265, 4189-4192.
20. + efflux from yeast cells expressing the mammalian sodium pump. Mol. Pharmacol. 45, 1132-1136.
21. Scheiner-Bobis, G., and Farley, R. A. (1994) Subunit requirements for expression of functional sodium pumps in yeast cells. Biochim. Biophys. Acta 1193, 226-234.
22. Wang, S. G., and Farley, R. A. (1998) Valine 904, tyrosine 898, and cysteine 908 in Na, K.-ATPase alpha subunits are important for assembly with beta subunits. J. Biol. Chem. 273, 29400-29405.
23. Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., and Erlich, H. A. (1988) Primerdirected enzymatic amplification of DNA with a thermostable DNA polymerase. Science 239, 487-491.
24. Hemsley, A., Arnheim, N., Toney, M. D., Cortopassi, G., and Galas, D. J. (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res. 17, 6545-6551.
25. Hitti, Y. S., and Bertino, A. M. (1994) Proteinase K and T4 DNA polymerase facilitate the blunt-end subcloning of PCR products. Biotechniques 16, 802-805.
26. 6-methylguanine lesions. J. Biol. Chem. 276, 24286-24292.
27. Dower, W. J., Miller, J. F., and Ragsdale, C. W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16, 6127-6145.
28. Potter, H. (1988) Electroporation in biology: methods, applications, and instrumentation. Anal. Biochem. 174, 361-373.
29. Cotrutz, C., Ionescu, C. R., Cotrutz, C. E., and Kocsis, M. M. (1995) DNA sequencing. Methods and computer analysis of sequence data. Part II. Rev. Med. Chir. Soc. Med. Nat. Iasi. 99, 17-21.
30. Gietz, R. D., Schiestl, R. H., Willems, A. R., and Woods, R. A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11, 355-360.
31. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
32. ,-ATPase. Toxicon 27, 1171-1187.
33. +-ATPase in rat colon. Eur. J. Biochem. 269, 3905-3911.
34. +)-ATPase preparations from different tissues and species. Determination of kinetic constants and dissociation constants. Biochim. Biophys. Acta 307, 386-398.
35. +)-activated ATPase. A biochemical link to digitalis-induced inotropy. Pharmacol. Rev. 36, 143-163.
36. +)-ATPase. J. Biol. Chem. 263, 235-242.
37. Anner, B. M., Moosmayer, M., and Imesch, E. (1994) Na, K.-ATPase characterized in artificial membranes. I. Predominant conformations and ion-fluxes associated with active and inhibited states. Mol. Membr. Biol. 11, 237-245.
38. +-ATPase. Naunyn-Schmiedeberg's Arch. Pharmacol. 325, 85-87.
39. +-ATPase does not require a catalytically active enzyme. Eur. J. Biochem. 248, 717-723.
40. +)-ATPase. Ligand interactions and related enzyme forms. Biochim. Biophys. Acta 821, 17-29.
41. +)-ATPase. Biochim. Biophys. Acta 727, 101-107.
42. 2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. Biochem. J. 339, 223-226.
43. 2 conformational change. Proc. Natl. Acad. Sci. U.S.A. 97, 11954-11959.
44. Koonin, E. V., and Tatusov, R. L. (1994) Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 244, 125-132.
45. +-ATPase deduced by restraint-based comparative modeling shows only one ATP-binding site. J. Mol. Model. 7, 184-192.
46. Wang, W., Kim, R., Jancarik, J., Yokota, H., and Kim, S. H. (2001) Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution. Structure (Camb) 9, 65-71.