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Volumn 391, Issue 5, 2009, Pages 858-871

High-yield Heterologous Expression of Wild Type and Mutant Ca2+ ATPase: Characterization of Ca2+ Binding Sites by Charge Transfer

Author keywords

charge transfer; heterologous expression; SERCA1

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; MAGNESIUM ION;

EID: 68349095078     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.044     Document Type: Article
Times cited : (20)

References (47)
  • 1
    • 0022371456 scopus 로고
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316 (1985) 696-700
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 2
    • 0018401053 scopus 로고
    • 2+-dependent ATPase of sarcoplasmic reticulum
    • 2+-dependent ATPase of sarcoplasmic reticulum. Annu. Rev. Biochem. 48 (1979) 275-292
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-292
    • de Meis, L.1    Vianna, A.L.2
  • 3
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • Kühlbrandt W. Biology, structure and mechanism of P-type ATPases. Nat. Rev. Mol. Cell. Biol. 5 (2004) 282-295
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 4
    • 0019320911 scopus 로고
    • Cooperative calcium binding and ATPase activation in sarcoplasmic reticulum vesicles
    • Inesi G., Kurzmack M., Coan C., and Lewis D.E. Cooperative calcium binding and ATPase activation in sarcoplasmic reticulum vesicles. J. Biol. Chem. 255 (1980) 3025-3031
    • (1980) J. Biol. Chem. , vol.255 , pp. 3025-3031
    • Inesi, G.1    Kurzmack, M.2    Coan, C.3    Lewis, D.E.4
  • 5
    • 0019331870 scopus 로고
    • Adenosine 5′-triphosphate dependent fluxes of manganese and hydrogen ions in sarcoplasmic reticulum vesicles
    • Chiesi M., and Inesi G. Adenosine 5′-triphosphate dependent fluxes of manganese and hydrogen ions in sarcoplasmic reticulum vesicles. Biochemistry 19 (1980) 2912-2918
    • (1980) Biochemistry , vol.19 , pp. 2912-2918
    • Chiesi, M.1    Inesi, G.2
  • 6
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen C., Sørensen T.L., Nielsen R.C., Møller J.V., and Nissen P. Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306 (2004) 2251-2255
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sørensen, T.L.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 8
    • 0015791798 scopus 로고
    • Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions
    • Masuda H., and de Meis L. Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions. Biochemistry 12 (1973) 4581-4585
    • (1973) Biochemistry , vol.12 , pp. 4581-4585
    • Masuda, H.1    de Meis, L.2
  • 9
    • 0027220837 scopus 로고
    • Functional consequences of alterations to hydrophobic amino acids located in the M4 transmembrane sector of the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Clarke D.M., Loo T.W., Rice W.J., Andersen J.P., Vilsen B., and MacLennan D.H. Functional consequences of alterations to hydrophobic amino acids located in the M4 transmembrane sector of the Ca(2+)-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 268 (1993) 18359-18364
    • (1993) J. Biol. Chem. , vol.268 , pp. 18359-18364
    • Clarke, D.M.1    Loo, T.W.2    Rice, W.J.3    Andersen, J.P.4    Vilsen, B.5    MacLennan, D.H.6
  • 10
    • 0028816888 scopus 로고
    • Structure-function relationships of cation translocation by Ca(2+)- and Na+, K(+)-ATPases studied by site-directed mutagenesis
    • Andersen J.P., and Vilsen B. Structure-function relationships of cation translocation by Ca(2+)- and Na+, K(+)-ATPases studied by site-directed mutagenesis. FEBS Lett. 359 (1995) 101-106
    • (1995) FEBS Lett. , vol.359 , pp. 101-106
    • Andersen, J.P.1    Vilsen, B.2
  • 11
    • 0032510833 scopus 로고    scopus 로고
    • Direct demonstration of Ca2+ binding defects in sarco-endoplasmic reticulum Ca2+ ATPase mutants overexpressed in COS-1 cells transfected with adenovirus vectors
    • Strock C., Cavagna M., Peiffer W.E., Sumbilla C., Lewis D., and Inesi G. Direct demonstration of Ca2+ binding defects in sarco-endoplasmic reticulum Ca2+ ATPase mutants overexpressed in COS-1 cells transfected with adenovirus vectors. J. Biol. Chem. 273 (1998) 15104-15109
    • (1998) J. Biol. Chem. , vol.273 , pp. 15104-15109
    • Strock, C.1    Cavagna, M.2    Peiffer, W.E.3    Sumbilla, C.4    Lewis, D.5    Inesi, G.6
  • 12
    • 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. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 14
    • 39649087584 scopus 로고    scopus 로고
    • The funnel approach to the Precrystallization production of membrane protein
    • Lewison O., Leen A.T., and Rees D.C. The funnel approach to the Precrystallization production of membrane protein. J. Mol. Biol. 377 (2007) 62-73
    • (2007) J. Mol. Biol. , vol.377 , pp. 62-73
    • Lewison, O.1    Leen, A.T.2    Rees, D.C.3
  • 15
    • 0036840148 scopus 로고    scopus 로고
    • Cooperative setting for long-range linkage of Ca(2+) binding and ATP synthesis in the Ca(2+) ATPase
    • Inesi G., Zhang Z., and Lewis D. Cooperative setting for long-range linkage of Ca(2+) binding and ATP synthesis in the Ca(2+) ATPase. Biophys. J. 83 (2002) 2327-2332
    • (2002) Biophys. J. , vol.83 , pp. 2327-2332
    • Inesi, G.1    Zhang, Z.2    Lewis, D.3
  • 16
    • 33947298937 scopus 로고
    • Theory of the measurements of weak molecular complexes. II. Consequences of multiple equilibria
    • Deranleau D.A. Theory of the measurements of weak molecular complexes. II. Consequences of multiple equilibria. J. Am. Chem. Soc. 91 (1969) 4050-4054
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 4050-4054
    • Deranleau, D.A.1
  • 18
    • 38149066061 scopus 로고    scopus 로고
    • 2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin
    • 2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin. J. Biol. Chem. 283 (2008) 1189-1196
    • (2008) J. Biol. Chem. , vol.283 , pp. 1189-1196
    • Inesi, G.1    Lewis, D.2    Toyoshima, C.3    Hirata, A.4    de Meis, L.5
  • 20
    • 0027242123 scopus 로고
    • Mutation of glutamate 309 to glutamine alters one Ca(2+)-binding site in the Ca(2+)-ATPase of sarcoplasmic reticulum expressed in Sf9 cells
    • Skerjanc I.S., Toyofuku T., Richardson C., and MacLennan D.H. Mutation of glutamate 309 to glutamine alters one Ca(2+)-binding site in the Ca(2+)-ATPase of sarcoplasmic reticulum expressed in Sf9 cells. J. Biol. Chem. 268 (1993) 15944-15950
    • (1993) J. Biol. Chem. , vol.268 , pp. 15944-15950
    • Skerjanc, I.S.1    Toyofuku, T.2    Richardson, C.3    MacLennan, D.H.4
  • 21
    • 1442289363 scopus 로고    scopus 로고
    • Improved expression a characterization of Ca2+-ATPase and phospholamban in High-Five Cells
    • Waggoner J.R., Huffman J., Griffith B.N., Jones L.R., and Mahaney J.E. Improved expression a characterization of Ca2+-ATPase and phospholamban in High-Five Cells. Protein Expr. Purif. 34 (2004) 56-67
    • (2004) Protein Expr. Purif. , vol.34 , pp. 56-67
    • Waggoner, J.R.1    Huffman, J.2    Griffith, B.N.3    Jones, L.R.4    Mahaney, J.E.5
  • 23
    • 3943055518 scopus 로고    scopus 로고
    • Structural basis of ion pumping by Ca2+-ATPase of the sarcoplasmic reticulum
    • Toyoshima C., and Inesi G. Structural basis of ion pumping by Ca2+-ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 73 (2004) 269-292
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 269-292
    • Toyoshima, C.1    Inesi, G.2
  • 25
    • 0036216873 scopus 로고    scopus 로고
    • 2+ interaction with the ion-binding sites of the SR Ca-ATPase
    • 2+ interaction with the ion-binding sites of the SR Ca-ATPase. Biophys. J. 82 (2002) 170-181
    • (2002) Biophys. J. , vol.82 , pp. 170-181
    • Peinelt, C.1    Apell, H.-J.2
  • 29
    • 0028310431 scopus 로고
    • A pK change of acidic residues contributes to cation countertransport in the Ca-ATPase of sarcoplasmic reticulum. Role of H+ in Ca(2+)-ATPase countertransport
    • Yu X., Hao L., and Inesi G. A pK change of acidic residues contributes to cation countertransport in the Ca-ATPase of sarcoplasmic reticulum. Role of H+ in Ca(2+)-ATPase countertransport. J. Biol. Chem. 269 (1994) 16656-16661
    • (1994) J. Biol. Chem. , vol.269 , pp. 16656-16661
    • Yu, X.1    Hao, L.2    Inesi, G.3
  • 31
    • 47049101464 scopus 로고    scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. Arch. Biochem. Biophys. 476 (2008) 3-11
    • (2008) Arch. Biochem. Biophys. , vol.476 , pp. 3-11
    • Toyoshima, C.1
  • 32
    • 0027522055 scopus 로고
    • Ca(2+)-dependent and thapsigargin-inhibited phosphorylation of Na+,K(+)-ATPase catalytic domain following chimeric recombination with Ca(2+)-ATPase
    • Sumbilla C., Lu L., Lewis D.E., Inesi G., Ishii T., Takeyasu K., et al. Ca(2+)-dependent and thapsigargin-inhibited phosphorylation of Na+,K(+)-ATPase catalytic domain following chimeric recombination with Ca(2+)-ATPase. J. Biol. Chem. 268 (1993) 21185-21192
    • (1993) J. Biol. Chem. , vol.268 , pp. 21185-21192
    • Sumbilla, C.1    Lu, L.2    Lewis, D.E.3    Inesi, G.4    Ishii, T.5    Takeyasu, K.6
  • 34
    • 33748201193 scopus 로고    scopus 로고
    • Efficient generation of double heterologous promoter controlled oncolytic adenovirus vectors by a single homologous recombination step in Escherichia coli
    • Hoffman D., and Wildner O. Efficient generation of double heterologous promoter controlled oncolytic adenovirus vectors by a single homologous recombination step in Escherichia coli. BMC Biotechnol. 6 (2006) 36-48
    • (2006) BMC Biotechnol. , vol.6 , pp. 36-48
    • Hoffman, D.1    Wildner, O.2
  • 35
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 36
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166 (1983) 557-580
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 37
    • 0017710978 scopus 로고
    • Characterization of a human cell line transformed by DNA from human adenovirus type 5
    • Graham F.L., Smiley J., Russel W.C., and Nairn R. Characterization of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36 (1977) 58-72
    • (1977) J. Gen. Virol. , vol.36 , pp. 58-72
    • Graham, F.L.1    Smiley, J.2    Russel, W.C.3    Nairn, R.4
  • 38
    • 0019351935 scopus 로고
    • SV40-transformed simian cells support the replication of early SV40 mutants
    • Gluzman Y. SV40-transformed simian cells support the replication of early SV40 mutants. Cell 23 (1981) 175-182
    • (1981) Cell , vol.23 , pp. 175-182
    • Gluzman, Y.1
  • 39
    • 0030905733 scopus 로고    scopus 로고
    • Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • Autry J.M., and Jones L.R. Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J. Biol. Chem. 272 (1997) 15872-15880
    • (1997) J. Biol. Chem. , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 40
    • 0015403570 scopus 로고
    • Phospholipid orientation in sarcoplasmic membranes: spin-label ESR and proton MNR studies
    • Eletr S., and Inesi G. Phospholipid orientation in sarcoplasmic membranes: spin-label ESR and proton MNR studies. Biochim. Biophys. Acta 282 (1972) 174-179
    • (1972) Biochim. Biophys. Acta , vol.282 , pp. 174-179
    • Eletr, S.1    Inesi, G.2
  • 42
    • 0033021364 scopus 로고    scopus 로고
    • +-ATPase investigated on solid supported membranes: rapid solution exchange with a new technique
    • +-ATPase investigated on solid supported membranes: rapid solution exchange with a new technique. Biophys. J. 76 (1999) 814-826
    • (1999) Biophys. J. , vol.76 , pp. 814-826
    • Pintschovius, J.1    Fendler, K.2
  • 43
    • 2942657752 scopus 로고    scopus 로고
    • Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATPase measured on a solid supported membrane
    • Tadini Buoninsegni F., Bartolommei G., Moncelli M.R., Inesi G., and Guidelli R. Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATPase measured on a solid supported membrane. Biophys J. 86 (2004) 3671-3686
    • (2004) Biophys J. , vol.86 , pp. 3671-3686
    • Tadini Buoninsegni, F.1    Bartolommei, G.2    Moncelli, M.R.3    Inesi, G.4    Guidelli, R.5
  • 47
    • 1642317185 scopus 로고    scopus 로고
    • Some precautions in using chelators to buffer metals in biological solutions
    • Patton C., Thompson S., and Epel D. Some precautions in using chelators to buffer metals in biological solutions. Cell Calcium 35 (2004) 427-431
    • (2004) Cell Calcium , vol.35 , pp. 427-431
    • Patton, C.1    Thompson, S.2    Epel, D.3


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