메뉴 건너뛰기




Volumn 45, Issue 10, 2006, Pages 3460-3471

TNP-8N3-ADP photoaffinity labeling of two Na,K-ATPase sequences under separate Na+ plus K+ control

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; RATE CONSTANTS; SODIUM;

EID: 33644901576     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051927k     Document Type: Article
Times cited : (5)

References (77)
  • 1
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • Kaplan, J. H. (2002) Biochemistry of Na,K-ATPase, Annu. Rev. Biochem. 77, 511-535.
    • (2002) Annu. Rev. Biochem. , vol.77 , pp. 511-535
    • Kaplan, J.H.1
  • 2
    • 0038621773 scopus 로고    scopus 로고
    • Structure and mechanism of Na,K-ATPase. Functional sites and their interactions
    • Jørgensen, P. L., Håkansson, K. O., and Karlish, S. J. D. (2003) Structure and mechanism of Na,K-ATPase. Functional sites and their interactions, Annu. Rev. Physiol. 65, 817-849.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 817-849
    • Jørgensen, P.L.1    Håkansson, K.O.2    Karlish, S.J.D.3
  • 4
    • 0018910453 scopus 로고
    • The order of release of sodium and addition of potassium in the sodium-potassium pump reaction mechanism
    • Sachs, J. R. (1980) The order of release of sodium and addition of potassium in the sodium-potassium pump reaction mechanism, J. Physiol. 302, 219-240.
    • (1980) J. Physiol. , vol.302 , pp. 219-240
    • Sachs, J.R.1
  • 5
    • 0019393876 scopus 로고
    • The interaction of potassium ions and ATP on the sodium pump of resealed ghosts
    • Eisner, D. A., and Richards, D. E. (1981) The interaction of potassium ions and ATP on the sodium pump of resealed ghosts, J. Physiol. 319, 403-418.
    • (1981) J. Physiol. , vol.319 , pp. 403-418
    • Eisner, D.A.1    Richards, D.E.2
  • 6
    • 0015218603 scopus 로고
    • Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase
    • Hegyvary, C., and Post, R. L. (1971) Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase, J. Biol. Chem. 246, 5234-5240.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5234-5240
    • Hegyvary, C.1    Post, R.L.2
  • 8
    • 0017598305 scopus 로고
    • Phosphorylation from adenosine triphosphate of sodium- and potassium-activated adenosine triphosphatase. Comparison of enzyme-ligand complexes as precursors to the phosphoenzyme
    • Mårdh, S., and Post, R. L. (1977) Phosphorylation from adenosine triphosphate of sodium- and potassium-activated adenosine triphosphatase. Comparison of enzyme-ligand complexes as precursors to the phosphoenzyme, J. Biol. Chem. 252, 633-638.
    • (1977) J. Biol. Chem. , vol.252 , pp. 633-638
    • Mårdh, S.1    Post, R.L.2
  • 9
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • 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.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 10
    • 0020002086 scopus 로고
    • Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport
    • Glynn, I. M., and Richards, D. E. (1982) Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport, J. Physiol. 330, 17-43.
    • (1982) J. Physiol. , vol.330 , pp. 17-43
    • Glynn, I.M.1    Richards, D.E.2
  • 11
    • 0023655684 scopus 로고
    • 86Rb from an occluded state of the Na,K-pump in the presence of ATP and ADP
    • 86Rb from an occluded state of the Na,K-pump in the presence of ATP and ADP, J. Biol. Chem. 262, 11104-11115.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11104-11115
    • Forbush III, B.1
  • 13
    • 0002591052 scopus 로고
    • +-transporting adenosine triphosphatase
    • (Martonosi, A. N., Ed.), Plenum Press, New York
    • +-transporting adenosine triphosphatase, in The Enzymes of Biological Membranes (Martonosi, A. N., Ed.) Vol. 3, pp 35-114, Plenum Press, New York.
    • (1985) The Enzymes of Biological Membranes , vol.3 , pp. 35-114
    • Glynn, I.M.1
  • 14
    • 0027254430 scopus 로고
    • Solubilized αβ Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP
    • Ward, D. G., and Cavieres, J. D. (1993) Solubilized αβ Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP, Proc. Natl. Acad. Sci. U.S.A. 90, 5338-5336.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5338-15336
    • Ward, D.G.1    Cavieres, J.D.2
  • 15
    • 0029893954 scopus 로고    scopus 로고
    • Binding of 2′(3′)-O-(2,4,6-trinitrophenyl)ADP to soluble αβ protomers of Na,K-ATPase modified with fluorescein isothiocyanate: Evidence for two distinct nucleotide sites
    • Ward, D. G., and Cavieres, J. D. (1996) Binding of 2′(3′)-O- (2,4,6-trinitrophenyl)ADP to soluble αβ protomers of Na,K-ATPase modified with fluorescein isothiocyanate: Evidence for two distinct nucleotide sites, J. Biol. Chem. 271, 12317-12321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12317-12321
    • Ward, D.G.1    Cavieres, J.D.2
  • 16
    • 0019052331 scopus 로고
    • Characterization of conformational changes in (Na,K)ATPase labeled with fluorescein at the active site
    • Karlish, S. J. D. (1980) Characterization of conformational changes in (Na,K)ATPase labeled with fluorescein at the active site, J. Bioenerg. Biomembr. 12, 111-136.
    • (1980) J. Bioenerg. Biomembr. , vol.12 , pp. 111-136
    • Karlish, S.J.D.1
  • 18
    • 0032486484 scopus 로고    scopus 로고
    • 3-ATP. Abolition of E1 and E2 partial reactions by sequential block of high and low-affinity nucleotide sites
    • 3-ATP. Abolition of E1 and E2 partial reactions by sequential block of high and low-affinity nucleotide sites, J. Biol. Chem. 273, 14277-14284.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14277-14284
    • Ward, D.G.1    Cavieres, J.D.2
  • 20
    • 0032509485 scopus 로고    scopus 로고
    • 32P]-ADP) as a photoactivatable probe. Label incorporation before and after blocking the high affinity ATP site with fluorescein isothiocyanate
    • 32P]-ADP) as a photoactivatable probe. Label incorporation before and after blocking the high affinity ATP site with fluorescein isothiocyanate, J. Biol. Chem. 273, 33759-33765.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33759-33765
    • Ward, D.G.1    Cavieres, J.D.2
  • 21
    • 0024794115 scopus 로고
    • ATP-driven cation pumps: Alignment of sequences
    • Green, N. M. (1989) ATP-driven cation pumps: Alignment of sequences, Biochem. Soc. Trans. 17, 970-972.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 970-972
    • Green, N.M.1
  • 22
    • 0034033869 scopus 로고    scopus 로고
    • 2+-ATPase defines a new domain structure
    • 2+-ATPase defines a new domain structure, Biophys. J. 78, 1765-1776.
    • (2000) Biophys. J. , vol.78 , pp. 1765-1776
    • Stokes, D.L.1    Green, N.M.2
  • 23
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • 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.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 24
    • 0016184723 scopus 로고
    • +)-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate
    • +)-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate, Biochim. Biophys. Acta 356, 36-52.
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 36-52
    • Jørgensen, P.L.1
  • 26
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H., and Subbarow, Y. (1925) The colorimetric determination of phosphorus, J. Biol. Chem. 66, 375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of protein in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of protein in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 30
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R., and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase, J. Biol. Chem. 237, 3245-3249.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 31
    • 0019497930 scopus 로고
    • Characterization of 2′,3′-O-(2,4,6- trinitrocyclohexadienylidine)adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP
    • Moczydlowsky, E. G., and Fortes, P. A. G. (1981) Characterization of 2′,3′-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP, J. Biol. Chem. 256, 2346-2356.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2346-2356
    • Moczydlowsky, E.G.1    Fortes, P.A.G.2
  • 39
    • 0028356961 scopus 로고
    • Photochemical labeling and inhibition of Na,K-ATPase by 2-azido-ATP. Identification of an amino acid located within the ATP binding site
    • Tran, C. M., Huston, E. E., and Farley, R. A. (1994) Photochemical labeling and inhibition of Na,K-ATPase by 2-azido-ATP. Identification of an amino acid located within the ATP binding site, J. Biol. Chem. 269, 6558-6565.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6558-6565
    • Tran, C.M.1    Huston, E.E.2    Farley, R.A.3
  • 40
    • 0021173423 scopus 로고
    • The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase
    • Parley, R. A., Tran, C. M., Carilli, C. T., Hawke, D., and Shively, J. E. (1984) The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase, J. Biol. Chem. 259, 9532-9535.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9532-9535
    • Parley, R.A.1    Tran, C.M.2    Carilli, C.T.3    Hawke, D.4    Shively, J.E.5
  • 41
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanisms revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H., and Tsuda, T. (2004) Lumenal gating mechanisms revealed in calcium pump crystal structures with phosphate analogues, Nature 432, 361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 42
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C., and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue, Nature 430, 529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 44
    • 0038352127 scopus 로고    scopus 로고
    • 4ATP binding at a low affinity site in the protomeric enzyme unit
    • 4ATP binding at a low affinity site in the protomeric enzyme unit, J. Biol. Chem. 278, 14688-14697.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14688-14697
    • Ward, D.G.1    Cavieres, J.D.2
  • 47
    • 0025101069 scopus 로고
    • The ATP binding site of the yeast plasma membrane proton-translocating ATPase
    • Davis, C. B., Smith, K. E., Campbell, B. N., Jr., and Hammes, G. G. (1990) The ATP binding site of the yeast plasma membrane proton-translocating ATPase, J. Biol. Chem. 265, 1300-1305.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1300-1305
    • Davis, C.B.1    Smith, K.E.2    Campbell Jr., B.N.3    Hammes, G.G.4
  • 48
    • 0026784847 scopus 로고
    • Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase
    • Wang, K., and Farley, R. A. (1992) Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase, J. Biol. Chem. 267, 3577-3580.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3577-3580
    • Wang, K.1    Farley, R.A.2
  • 50
    • 0037133230 scopus 로고    scopus 로고
    • Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase
    • Hua, S., Ma, H., Lewis, D., Inesi, G., and Toyoshima, C. (2002) Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase, Biochemistry 41, 2264-2272.
    • (2002) Biochemistry , vol.41 , pp. 2264-2272
    • Hua, S.1    Ma, H.2    Lewis, D.3    Inesi, G.4    Toyoshima, C.5
  • 52
    • 0031890075 scopus 로고    scopus 로고
    • +-ATPase, at Lys-501 of the α-chain, accepts ATP independent of pyridoxal 5′-diphospho-5′-adenosine modification at Lys-480
    • +-ATPase, at Lys-501 of the α-chain, accepts ATP independent of pyridoxal 5′-diphospho-5′-adenosine modification at Lys-480, J. Biochem. 123, 169-174.
    • (1998) J. Biochem. , vol.123 , pp. 169-174
    • Tsuda, T.1    Kaya, S.2    Funatsu, H.3    Hayashi, Y.4    Taniguchi, K.5
  • 53
    • 0034637552 scopus 로고    scopus 로고
    • +-ATPase, nor do the sites coexist in native enzyme
    • +-ATPase, nor do the sites coexist in native enzyme, J. Biol. Chem. 275, 24512.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24512
    • Martin, D.1    Sachs, J.R.2
  • 56
    • 0022486250 scopus 로고
    • +-transporting ATPase: Location of the 5′-(p-fluorosulfonyl)bezoyladenosine binding site and soluble peptides released by trypsin
    • +-transporting ATPase: Location of the 5′-(p-fluorosulfonyl)bezoyladenosine binding site and soluble peptides released by trypsin, Proc. Natl. Acad. Sci. U.S.A. 83, 2071-2075.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2071-2075
    • Ohta, T.1    Nagano, K.2    Yoshida, M.3
  • 59
    • 0020479618 scopus 로고
    • The use of 2′,3′-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate for studies of nucleotide interaction with sarcoplasmic reticulum vesicles
    • Watanabe, T., and Inesi, G. (1982) The use of 2′,3′-O-(2,4,6- trinitrophenyl) adenosine 5′-triphosphate for studies of nucleotide interaction with sarcoplasmic reticulum vesicles, J. Biol. Chem. 257, 11510-11516.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11510-11516
    • Watanabe, T.1    Inesi, G.2
  • 61
    • 0024964932 scopus 로고
    • +-ATPase: Evidence for two classes of nucleotide sites
    • +-ATPase: Evidence for two classes of nucleotide sites, Biochemistry 28, 6771-6778.
    • (1989) Biochemistry , vol.28 , pp. 6771-6778
    • Faller, L.D.1
  • 62
    • 0016786376 scopus 로고
    • +)-ATPase. V. Conformational changes in the enzyme transitions between the Na-form and the K-form studied with tryptic digestion as a tool
    • +)-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.
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 399-415
    • Jørgensen, P.L.1
  • 64
    • 0023028790 scopus 로고
    • Conformational transitions in fluorescein-labeled (Na,K)ATPase reconstituted into phospholipid vesicles
    • Rephaeli, A., Richards, D., and Karlish, S. J. D. (1986) Conformational transitions in fluorescein-labeled (Na,K)ATPase reconstituted into phospholipid vesicles, J. Biol. Chem. 261, 6248-6254.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6248-6254
    • Rephaeli, A.1    Richards, D.2    Karlish, S.J.D.3
  • 67
    • 0037155140 scopus 로고    scopus 로고
    • +-ATPase. I. The identity of occluded states formed by the physiological route or the direct routes: Occlusion/deocclusion kinetics through the direct route
    • +-ATPase. I. The identity of occluded states formed by the physiological route or the direct routes: Occlusion/deocclusion kinetics through the direct route, J. Biol. Chem. 277, 5910-5921.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5910-5921
    • González-Lebrero, R.M.1    Kaufman, S.B.2    Montes, M.R.3    Nørby, J.4    Garrahan, P.J.5    Rossi, R.C.6
  • 68
    • 0015635255 scopus 로고
    • The interaction of sodium and potassium with the sodium pump in red cells
    • Garay, R. P., and Garrahan, P. J. (1973) The interaction of sodium and potassium with the sodium pump in red cells, J. Physiol. 231, 297-325.
    • (1973) J. Physiol. , vol.231 , pp. 297-325
    • Garay, R.P.1    Garrahan, P.J.2
  • 69
    • 0023905892 scopus 로고
    • +)-ATPase: Pertinence of the adenine and fluorescein binding sites
    • +)-ATPase: Pertinence of the adenine and fluorescein binding sites, Biochim. Biophys. Acta 953, 26-36.
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 26-36
    • Davis, R.L.1    Robinson, J.D.2
  • 70
    • 0020397382 scopus 로고
    • Sodium pump-mediated ATP:ADP exchange. The sided effects of sodium and potassium ions
    • Kaplan, J. H. (1982) Sodium pump-mediated ATP:ADP exchange. The sided effects of sodium and potassium ions, J. Gen. Physiol. 80, 915-937.
    • (1982) J. Gen. Physiol. , vol.80 , pp. 915-937
    • Kaplan, J.H.1
  • 71
    • 0016734238 scopus 로고
    • Allosteric inhibition of the sodium pump by external sodium
    • Cavieres, J. D., and Ellory, J. C. (1975) Allosteric inhibition of the sodium pump by external sodium, Nature 255, 338-340.
    • (1975) Nature , vol.255 , pp. 338-340
    • Cavieres, J.D.1    Ellory, J.C.2
  • 72
    • 0023813373 scopus 로고
    • 2 conformational transitions in Na,K-pump and Ca-pump proteins
    • 2 conformational transitions in Na,K-pump and Ca-pump proteins, J. Membr. Biol. 103, 95-120.
    • (1988) J. Membr. Biol. , vol.103 , pp. 95-120
    • Jørgensen, P.L.1    Andersen, J.P.2
  • 75
    • 0020001045 scopus 로고
    • Passive rubidium fluxes mediated by Na,K-ATPase reconstituted into phospholipid vesicles when ATP- and phosphate-free
    • Karlish, S. J. D., and Stein, W. D. (1982) Passive rubidium fluxes mediated by Na,K-ATPase reconstituted into phospholipid vesicles when ATP- and phosphate-free, J. Physiol. 328, 295-316.
    • (1982) J. Physiol. , vol.328 , pp. 295-316
    • Karlish, S.J.D.1    Stein, W.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.