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Volumn 44, Issue 8, 2005, Pages 3101-3111

Structural investigation into the differential target enzyme regulation displayed by plant calmodulin isoforms

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; CHEMICAL ACTIVATION; CHEMICAL BONDS; ENZYME INHIBITION; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLANTS (BOTANY); THERMODYNAMICS; TITRATION;

EID: 14344261396     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047770y     Document Type: Article
Times cited : (28)

References (48)
  • 1
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D., and Means, A. R. (2000) Calmodulin: a prototypical calcium sensor, Trends Cell Biol. 10, 322-328.
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 2
    • 0034945001 scopus 로고    scopus 로고
    • Calmodulin as a versatile calcium signal transducer in plants
    • Snedden, W. A., and Fromm, H. (2001) Calmodulin as a versatile calcium signal transducer in plants, New Phytol. 151, 35-66.
    • (2001) New Phytol. , vol.151 , pp. 35-66
    • Snedden, W.A.1    Fromm, H.2
  • 5
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin, Nat. Struct. Biol. 2, 758-767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 6
    • 0031041379 scopus 로고    scopus 로고
    • Functional consequences of truncating amino acid side chains located at a calmodulin-peptide interface
    • Chin, D., Sloan, D. J., Quiocho, F. A., and Means, A. R. (1997) Functional consequences of truncating amino acid side chains located at a calmodulin-peptide interface, J. Biol. Chem. 272, 5510-5513.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5510-5513
    • Chin, D.1    Sloan, D.J.2    Quiocho, F.A.3    Means, A.R.4
  • 7
    • 0034235139 scopus 로고    scopus 로고
    • Spectroscopic characterization of the interaction between calmodulin- dependent protein kinase I and calmodulin
    • Gomes, A. V., Barnes, J. A., and Vogel, H. J. (2000) Spectroscopic characterization of the interaction between calmodulin- dependent protein kinase I and calmodulin, Arch. Biochem. Biophys. 379, 28-36.
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 28-36
    • Gomes, A.V.1    Barnes, J.A.2    Vogel, H.J.3
  • 8
    • 0037053380 scopus 로고    scopus 로고
    • A direct test of the reductionist approach to structural studies of calmodulin activity: Relevance of peptide models of target proteins
    • Kranz, J. K., Lee, E. K., Nairn, A. C., and Wand, A. J. (2002) A direct test of the reductionist approach to structural studies of calmodulin activity: relevance of peptide models of target proteins, J. Biol. Chem. 277, 16351-16354.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16351-16354
    • Kranz, J.K.1    Lee, E.K.2    Nairn, A.C.3    Wand, A.J.4
  • 9
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K. P. and Ikura, M. (2002) Calmodulin in action: diversity in target recognition and activation mechanisms, Cell 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 10
    • 4143076230 scopus 로고    scopus 로고
    • Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding
    • in press
    • Ishida, H. and Vogel, H. J. (2005) Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding, Protein Pept. Lett. (in press).
    • (2005) Protein Pept. Lett.
    • Ishida, H.1    Vogel, H.J.2
  • 11
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter, S. W., and Leclerc, E. (2003) Novel aspects of calmodulin target recognition and activation, Eur. J. Biochem. 270, 404-414.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 12
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk, A. P., and Vogel, H. J. (2004) Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides, Mol. Biotechnol. 27, 33-57.
    • (2004) Mol. Biotechnol. , vol.27 , pp. 33-57
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 13
    • 0037138403 scopus 로고    scopus 로고
    • Calmodulin signaling via the IQ motif
    • Bahler, M., and Rhoads, A. (2002) Calmodulin signaling via the IQ motif, FEBS Lett. 513, 107-113.
    • (2002) FEBS Lett. , vol.513 , pp. 107-113
    • Bahler, M.1    Rhoads, A.2
  • 15
    • 0032506166 scopus 로고    scopus 로고
    • Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
    • Cho, M. J., Vaghy, P. L., Kondo, R., Lee, S. H., Davis, J. P., Rehl, R., Heo, W. D., and Johnson, J. D. (1998) Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms, Biochemistry 37, 15593-15597.
    • (1998) Biochemistry , vol.37 , pp. 15593-15597
    • Cho, M.J.1    Vaghy, P.L.2    Kondo, R.3    Lee, S.H.4    Davis, J.P.5    Rehl, R.6    Heo, W.D.7    Johnson, J.D.8
  • 16
    • 0029101746 scopus 로고
    • Identification of a novel divergent calmodulin isoform from soybean which has differential ability to activate calmodulin-dependent enzymes
    • Lee, S. H., Kim, J. C., Lee, M. S., Heo, W. D., Seo, H. Y., Yoon, H. W., Hong, J. C., Lee, S. Y., Bahk, J. D., Hwang, I., and Cho, M. J. (1995) Identification of a novel divergent calmodulin isoform from soybean which has differential ability to activate calmodulin-dependent enzymes, J. Biol. Chem. 270, 21806-21812.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21806-21812
    • Lee, S.H.1    Kim, J.C.2    Lee, M.S.3    Heo, W.D.4    Seo, H.Y.5    Yoon, H.W.6    Hong, J.C.7    Lee, S.Y.8    Bahk, J.D.9    Hwang, I.10    Cho, M.J.11
  • 19
    • 0033579561 scopus 로고    scopus 로고
    • A point mutation in a plant calmodulin is responsible for its inhibition of nitric-oxide synthase
    • Kondo, R., Tikunova, S. B., Cho, M. J., and Johnson, J. D. (1999) A point mutation in a plant calmodulin is responsible for its inhibition of nitric-oxide synthase, J. Biol. Chem. 274, 36213-36218.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36213-36218
    • Kondo, R.1    Tikunova, S.B.2    Cho, M.J.3    Johnson, J.D.4
  • 22
    • 0037307080 scopus 로고    scopus 로고
    • Protein conformational changes studied by diffusion NMR spectroscopy: Application to helix-loop-helix calcium binding proteins
    • Weljie, A. M., Yamniuk, A. P., Yoshino, H., Izumi, Y., and Vogel, H. J. (2003) Protein conformational changes studied by diffusion NMR spectroscopy: application to helix-loop-helix calcium binding proteins, Protein Sci. 12, 228-236.
    • (2003) Protein Sci. , vol.12 , pp. 228-236
    • Weljie, A.M.1    Yamniuk, A.P.2    Yoshino, H.3    Izumi, Y.4    Vogel, H.J.5
  • 23
    • 0033514432 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the calmodulin- binding domain of cyclic nucleotide phosphodiesterase with calmodulin
    • Yuan, T., Walsh, M. P., Sutherland, C., Fabian, H., and Vogel, H. J. (1999) Calcium-dependent and -independent interactions of the calmodulin- binding domain of cyclic nucleotide phosphodiesterase with calmodulin, Biochemistry 38, 1446-1455.
    • (1999) Biochemistry , vol.38 , pp. 1446-1455
    • Yuan, T.1    Walsh, M.P.2    Sutherland, C.3    Fabian, H.4    Vogel, H.J.5
  • 24
    • 1542350090 scopus 로고    scopus 로고
    • Structurally homologous binding of plant calmodulin isoforms to the calmodulin-binding domain of vacuolar calcium-ATPase
    • Yamniuk, A. P., and Vogel, H. J. (2004) Structurally homologous binding of plant calmodulin isoforms to the calmodulin-binding domain of vacuolar calcium-ATPase, J. Biol. Chem. 279, 7698-7707.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7698-7707
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 25
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., and Braun, W. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules, J. Comput. Chem. 19, 319-333,
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 26
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce, M. M., Raman, C. S., and Nall, B. T. (1999) Isothermal titration calorimetry of protein-protein interactions, Methods 19, 213-221.
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 27
    • 0033605726 scopus 로고    scopus 로고
    • Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study
    • Yuan, T., Ouyang, H., and Vogel, H. J. (1999) Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study, J. Biol. Chem. 274, 8411-8420.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8411-8420
    • Yuan, T.1    Ouyang, H.2    Vogel, H.J.3
  • 28
    • 0025153333 scopus 로고
    • NMR identification of protein surfaces using paramagnetic probes
    • Petros, A. M., Mueller, L., and Kopple, K. D. (1990) NMR identification of protein surfaces using paramagnetic probes, Biochemistry 29, 10041-10048.
    • (1990) Biochemistry , vol.29 , pp. 10041-10048
    • Petros, A.M.1    Mueller, L.2    Kopple, K.D.3
  • 29
    • 0028673539 scopus 로고
    • Nuclear magnetic resonance methods for studying protein-ligand complexes
    • Petros, A. M. and Fesik, S. W. (1994) Nuclear magnetic resonance methods for studying protein-ligand complexes, Methods Enzymol. 239, 717-739.
    • (1994) Methods Enzymol. , vol.239 , pp. 717-739
    • Petros, A.M.1    Fesik, S.W.2
  • 30
    • 0029113770 scopus 로고
    • Interaction of calmodulin with its binding domain of rat cerebellar nitric oxide synthase. A multinuclear NMR study
    • Zhang, M., Yuan, T., Aramini, J. M., and Vogel, H. J. (1995) Interaction of calmodulin with its binding domain of rat cerebellar nitric oxide synthase. A multinuclear NMR study, J. Biol. Chem. 270, 20901-20907.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20901-20907
    • Zhang, M.1    Yuan, T.2    Aramini, J.M.3    Vogel, H.J.4
  • 31
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador, W. E., Means, A. R., and Quiocho, F. A. (1993) Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures, Science 262, 1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 32
    • 0031567108 scopus 로고    scopus 로고
    • Energetics of target peptide recognition by calmodulin: A calorimetric study
    • Wintrode, P. L., and Privalov, P. L. (1997) Energetics of target peptide recognition by calmodulin: a calorimetric study, J. Mol. Biol. 266, 1050-1062.
    • (1997) J. Mol. Biol. , vol.266 , pp. 1050-1062
    • Wintrode, P.L.1    Privalov, P.L.2
  • 33
    • 0035958004 scopus 로고    scopus 로고
    • Energetics of target peptide binding by calmodulin reveals different modes of binding
    • Brokx, R. D., Lopez, M. M., Vogel, H. J., and Makhatadze, G. I. (2001) Energetics of target peptide binding by calmodulin reveals different modes of binding, J. Biol. Chem. 276, 14083-14091.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14083-14091
    • Brokx, R.D.1    Lopez, M.M.2    Vogel, H.J.3    Makhatadze, G.I.4
  • 34
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink, M. R., Anusiem, A. C., and Biltonen, R. L. (1983) Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A, Biochemistry 22, 3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 35
    • 0034971963 scopus 로고    scopus 로고
    • Heat capacity changes upon burial of polar and nonpolar groups in proteins
    • Loladze, V. V., Ermolenko, D. N., and Makhatadze, G. I. (2001) Heat capacity changes upon burial of polar and nonpolar groups in proteins, Protein Sci. 10, 1343-1352.
    • (2001) Protein Sci. , vol.10 , pp. 1343-1352
    • Loladze, V.V.1    Ermolenko, D.N.2    Makhatadze, G.I.3
  • 36
    • 0022429037 scopus 로고
    • Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering
    • Seaton, B. A., Head, J. F., Engelman, D. M., and Richards, F. M. (1985) Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering, Biochemistry 24, 6740-6743.
    • (1985) Biochemistry , vol.24 , pp. 6740-6743
    • Seaton, B.A.1    Head, J.F.2    Engelman, D.M.3    Richards, F.M.4
  • 37
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • Aoyagi, M., Arvai, A. S., Tainer, J. A., and Getzoff, E. D. (2003) Structural basis for endothelial nitric oxide synthase binding to calmodulin, EMBO J. 22, 766-775.
    • (2003) EMBO J. , vol.22 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 38
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador, W. E., Means, A. R., and Quiocho, F. A. (1992) Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex, Science 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 39
    • 0036708456 scopus 로고    scopus 로고
    • Dynamic light scattering study of calmodulin-target peptide complexes
    • Papish, A. L., Tari, L. W., and Vogel, H. J. (2002) Dynamic light scattering study of calmodulin-target peptide complexes, Biophys. J. 83, 1455-1464.
    • (2002) Biophys. J. , vol.83 , pp. 1455-1464
    • Papish, A.L.1    Tari, L.W.2    Vogel, H.J.3
  • 41
    • 0034681952 scopus 로고    scopus 로고
    • The whole is not the simple sum of its parts in calmodulin from S. cerevisiae
    • Lee, S. Y., and Klevit, R. E. (2000) The whole is not the simple sum of its parts in calmodulin from S. cerevisiae, Biochemistry 39, 4225-4230.
    • (2000) Biochemistry , vol.39 , pp. 4225-4230
    • Lee, S.Y.1    Klevit, R.E.2
  • 42
    • 0030051180 scopus 로고    scopus 로고
    • Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: Implications for structure/function
    • Yoshino, H., Izumi, Y., Sakai, K., Takezawa, H., Matsuura, I., Maekawa, H., and Yazawa, M. (1996) Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: implications for structure/function, Biochemistry 35, 2388-2393.
    • (1996) Biochemistry , vol.35 , pp. 2388-2393
    • Yoshino, H.1    Izumi, Y.2    Sakai, K.3    Takezawa, H.4    Matsuura, I.5    Maekawa, H.6    Yazawa, M.7
  • 43
    • 0027493764 scopus 로고
    • Mutagenesis of the fourth calcium-binding domain of yeast calmodulin
    • Matsuura, I., Kimura, E., Tai, K., and Yazawa, M. (1993) Mutagenesis of the fourth calcium-binding domain of yeast calmodulin, J. Biol. Chem. 268, 13267-13273.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13267-13273
    • Matsuura, I.1    Kimura, E.2    Tai, K.3    Yazawa, M.4
  • 44
    • 0023429054 scopus 로고
    • Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae
    • Ohya, Y., Uno, I., Ishikawa, T., and Anraku, Y. (1987) Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae, Eur. J. Biochem. 168, 13-19.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 13-19
    • Ohya, Y.1    Uno, I.2    Ishikawa, T.3    Anraku, Y.4
  • 45
    • 0038740645 scopus 로고    scopus 로고
    • The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex
    • Chandok, M. R., Ytterberg, A. J., van Wijk, K. J., and Klessig, D. F. (2003) The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex, Cell 113, 469-482.
    • (2003) Cell , vol.113 , pp. 469-482
    • Chandok, M.R.1    Ytterberg, A.J.2    Van Wijk, K.J.3    Klessig, D.F.4
  • 46
    • 4544275715 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II produce opposing effects on the affinity of calmodulin for calcium
    • 2+/calmodulin-dependent protein kinase II produce opposing effects on the affinity of calmodulin for calcium, J. Biol. Chem. 279, 39374-39382.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39374-39382
    • Gaertner, T.R.1    Putkey, J.A.2    Waxham, M.N.3
  • 47
    • 0037046993 scopus 로고    scopus 로고
    • Target recognition of apocalmodulin by nitric oxide synthase I peptides
    • Censarek, P., Beyermann, M., and Koch, K. W. (2002) Target recognition of apocalmodulin by nitric oxide synthase I peptides, Biochemistry 41, 8598-8604.
    • (2002) Biochemistry , vol.41 , pp. 8598-8604
    • Censarek, P.1    Beyermann, M.2    Koch, K.W.3
  • 48
    • 8844286847 scopus 로고    scopus 로고
    • Thermodynamics of apocalmodulin and nitric oxide synthase II peptide interaction
    • Censarek, P., Beyermann, M., and Koch, K. W. (2004) Thermodynamics of apocalmodulin and nitric oxide synthase II peptide interaction, FEBS Lett. 577, 465-468.
    • (2004) FEBS Lett. , vol.577 , pp. 465-468
    • Censarek, P.1    Beyermann, M.2    Koch, K.W.3


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