메뉴 건너뛰기




Volumn 17, Issue 3, 2012, Pages 159-172

Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALCINEURIN; CALCIUM; CALMODULIN;

EID: 84857238843     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2012.01580.x     Document Type: Article
Times cited : (16)

References (60)
  • 1
    • 36749024011 scopus 로고    scopus 로고
    • The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains
    • Ataman, Z.A., Gakhar, L., Sorensen, B.R., Hell, J.W. & Shea, M.A. (2007) The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains. Structure 15, 1603-1617.
    • (2007) Structure , vol.15 , pp. 1603-1617
    • Ataman, Z.A.1    Gakhar, L.2    Sorensen, B.R.3    Hell, J.W.4    Shea, M.A.5
  • 3
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 4
    • 33846794573 scopus 로고    scopus 로고
    • The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex
    • Candel, A.M., Conejero-Lara, F., Martinez, J.C., van Nuland, N.A.J. & Bruix, M. (2007) The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex. FEBS Lett. 581, 687-692.
    • (2007) FEBS Lett. , vol.581 , pp. 687-692
    • Candel, A.M.1    Conejero-Lara, F.2    Martinez, J.C.3    van Nuland, N.A.J.4    Bruix, M.5
  • 6
    • 0004231403 scopus 로고
    • Amsterdam, the Netherlands: Elsevier
    • Cohen, P. & Klee, C.B. (1988) Calmodulin. Amsterdam, the Netherlands: Elsevier.
    • (1988) Calmodulin
    • Cohen, P.1    Klee, C.B.2
  • 7
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 8
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A. & Ikura, M. (1995) Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 9
    • 0035675838 scopus 로고    scopus 로고
    • Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae
    • Cyert, M. (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu. Rev. Genet. 35, 647-672.
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 647-672
    • Cyert, M.1
  • 10
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: calmodulin is an essential protein
    • Davis, T.N., Urdea, M.S., Masiarz, F.R. & Thorner, J. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47, 423-431.
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 11
  • 14
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • Frederick, K.K., Marlow, M.S., Valentine, K.G. & Wand, A.J. (2007) Conformational entropy in molecular recognition by proteins. Nature 448, 325-329.
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 18
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P. & Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 19
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: diversity in target recognition and activation mechanism
    • Hoeflich, K.P. & Ikura, M. (2002) Calmodulin in action: diversity in target recognition and activation mechanism. Cell 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 20
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. & Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 23
    • 0000739195 scopus 로고
    • Melittin binding causes a large calcium-dependent conformational change in calmodulin
    • Kataoka, M., Head, J.F., Seaton, B.A. & Engelman, D.M. (1989) Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proc. Natl Acad. Sci. USA 86, 6944-6948.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6944-6948
    • Kataoka, M.1    Head, J.F.2    Seaton, B.A.3    Engelman, D.M.4
  • 24
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger, C.R., Parge, H.E., Knighton, D.R., et al. (1995) Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 378, 641-644.
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1    Parge, H.E.2    Knighton, D.R.3
  • 25
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M.B. & Svergun, D.I. (2000) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41.
    • (2000) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 26
    • 0016908119 scopus 로고
    • Calcium-binding proteins
    • Kretsinger, R.H. (1976) Calcium-binding proteins. Annu. Rev. Biochem. 45, 239-266.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 239-266
    • Kretsinger, R.H.1
  • 27
    • 0028545648 scopus 로고
    • Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kuboniwa, H., Grzesiek, S., Delaglio, F. & Bax, A. (1994) Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4, 871-878.
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 29
    • 0034681952 scopus 로고    scopus 로고
    • The whole is not the simple sum of its parts in calmodulin from S. cerevisiae
    • Lee, S.Y. & 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
  • 30
    • 0023478561 scopus 로고
    • Yeast calmodulin: structural and functional differences compared with vertebrate calmodulin
    • Luan, Y., Matsuura, I., Yazawa, M., Nakamura, T. & Yagi, K. (1987) Yeast calmodulin: structural and functional differences compared with vertebrate calmodulin. J. Biochem. 102, 1531-1537.
    • (1987) J. Biochem. , vol.102 , pp. 1531-1537
    • Luan, Y.1    Matsuura, I.2    Yazawa, M.3    Nakamura, T.4    Yagi, K.5
  • 31
    • 65549147594 scopus 로고    scopus 로고
    • Domain swapping and different oligomeric States for the complex between calmodulin and the calmodulin-binding domain of calcineurin A
    • Majava, V. & Kursula, P. (2009) Domain swapping and different oligomeric States for the complex between calmodulin and the calmodulin-binding domain of calcineurin A. PLoS ONE 4, e5402.
    • (2009) PLoS ONE , vol.4
    • Majava, V.1    Kursula, P.2
  • 32
    • 34547557341 scopus 로고    scopus 로고
    • Functional silencing of TATA-binding protein (TBP) by a covalent linkage of the N-terminal domain of TBP-associated factor 1
    • Mal, T.K., Takahata, S., Ki, S., Zheng, L., Kokubo, T. & Ikura, M. (2007) Functional silencing of TATA-binding protein (TBP) by a covalent linkage of the N-terminal domain of TBP-associated factor 1. J. Biol. Chem. 282, 22228-22238.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22228-22238
    • Mal, T.K.1    Takahata, S.2    Ki, S.3    Zheng, L.4    Kokubo, T.5    Ikura, M.6
  • 34
    • 34548486475 scopus 로고    scopus 로고
    • Automatic maximum entropy spectral reconstruction in NMR
    • Mobli, M., Maciejewski, M.W., Gryk, M.R. & Hoch, J.C. (2007) Automatic maximum entropy spectral reconstruction in NMR. J. Biomol. NMR 39, 133-139.
    • (2007) J. Biomol. NMR , vol.39 , pp. 133-139
    • Mobli, M.1    Maciejewski, M.W.2    Gryk, M.R.3    Hoch, J.C.4
  • 35
    • 0033524458 scopus 로고    scopus 로고
    • Calcium binding induces interaction between the N- and C-terminal domains of yeast calmodulin and modulates its overall conformation
    • Nakashima, K., Ishida, H., Ohki, S., Hikichi, K. & Yazawa, M. (1999) Calcium binding induces interaction between the N- and C-terminal domains of yeast calmodulin and modulates its overall conformation. Biochemistry 38, 98-104.
    • (1999) Biochemistry , vol.38 , pp. 98-104
    • Nakashima, K.1    Ishida, H.2    Ohki, S.3    Hikichi, K.4    Yazawa, M.5
  • 36
    • 79551474570 scopus 로고    scopus 로고
    • Recognition of β-calcineurin by the domains of calmodulin: thermodynamic and structural evidence for distinct roles
    • O'Donnell, S.E., Yu, L., Fowler, C.A. & Shea, M.A. (2011) Recognition of β-calcineurin by the domains of calmodulin: thermodynamic and structural evidence for distinct roles. Proteins 79, 765-786.
    • (2011) Proteins , vol.79 , pp. 765-786
    • O'Donnell, S.E.1    Yu, L.2    Fowler, C.A.3    Shea, M.A.4
  • 37
    • 0023429054 scopus 로고
    • Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae
    • Ohya, Y., Uno, I., Ishikawa, T. & 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
  • 38
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices
    • O'Neil, K.T. & DeGrado, W.F. (1990) How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices. Trends Biochem. Sci. 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 39
    • 0028181021 scopus 로고
    • A calmodulin-target peptide hybrid molecule with unique calcium-binding properties
    • Porumb, T., Yau, P., Harvey, T.S. & Ikura, M. (1994) A calmodulin-target peptide hybrid molecule with unique calcium-binding properties. Protein Eng. 7, 109-115.
    • (1994) Protein Eng. , vol.7 , pp. 109-115
    • Porumb, T.1    Yau, P.2    Harvey, T.S.3    Ikura, M.4
  • 41
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads, A.R. & Friedberg, F. (1997) Sequence motifs for calmodulin recognition. FASEB J. 11, 331-340.
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 42
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: form and function
    • Rusnak, F. & Mertz, P. (2000) Calcineurin: form and function. Physiol. Rev. 80, 1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 43
  • 44
    • 0027286454 scopus 로고
    • Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae
    • Starovasnik, M.A., Davis, K.N. & Klevit, R.E. (1993) Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32, 3261-3270.
    • (1993) Biochemistry , vol.32 , pp. 3261-3270
    • Starovasnik, M.A.1    Davis, K.N.2    Klevit, R.E.3
  • 45
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D.I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 46
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D.I., Barberato, C. & Koch, M.H.J. (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 47
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D.I., Petoukhov, M.V. & Koch, M.H.J. (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 48
    • 0026750290 scopus 로고
    • The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains
    • Trewhella, J. (1992) The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. Cell Calcium 13, 377-390.
    • (1992) Cell Calcium , vol.13 , pp. 377-390
    • Trewhella, J.1
  • 49
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter, S.W. & 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
  • 50
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V. & Svergun, D.I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 51
    • 0033660312 scopus 로고    scopus 로고
    • Large-scale shape changes in proteins and macromolecular complexes
    • Wall, M.E., Gallagher, S.C. & Trewhella, J. (2000) Large-scale shape changes in proteins and macromolecular complexes. Annu. Rev. Phys. Chem. 51, 355-380.
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 355-380
    • Wall, M.E.1    Gallagher, S.C.2    Trewhella, J.3
  • 52
    • 0017101727 scopus 로고
    • 2+-and protein modulator-activated cyclic nucleotide phosphodiesterase
    • 2+-and protein modulator-activated cyclic nucleotide phosphodiesterase. Biochem. Biophys. Res. Commun. 72, 926-932.
    • (1976) Biochem. Biophys. Res. Commun. , vol.72 , pp. 926-932
    • Wang, J.H.1    Desai, R.2
  • 53
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk, A.P. & 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
  • 55
    • 0023655683 scopus 로고
    • Communication between two globular domains of calmodulin in the presence of mastoparan or caldesmon fragment
    • Yazawa, M., Ikura, M., Hikichi, K., Ying, L. & Yagi, K. (1987) Communication between two globular domains of calmodulin in the presence of mastoparan or caldesmon fragment. J. Biol. Chem. 262, 10951-10954.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10951-10954
    • Yazawa, M.1    Ikura, M.2    Hikichi, K.3    Ying, L.4    Yagi, K.5
  • 57
    • 50849094272 scopus 로고    scopus 로고
    • The complex structure of calmodulin bound to calcineurin peptide
    • Ye, Q., Wang, H., Zheng, J., Wei, Q. & Jia, Z. (2008) The complex structure of calmodulin bound to calcineurin peptide. Proteins 73, 19-27.
    • (2008) Proteins , vol.73 , pp. 19-27
    • Ye, Q.1    Wang, H.2    Zheng, J.3    Wei, Q.4    Jia, Z.5
  • 58
    • 0030051180 scopus 로고    scopus 로고
    • Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: implication for structure/function
    • Yoshino, H., Izumi, Y., Sakai, K., Takezawa, H., Matsuura, I., Maekawa, H. & Yazawa, M. (1996) Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: implication 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
  • 59
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T. & 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
  • 60
    • 47649120815 scopus 로고    scopus 로고
    • Ligand-induced dimer formation of calmodulin
    • Zhang, Y., Tan, H., Jia, Z. & Chen, G. (2008) Ligand-induced dimer formation of calmodulin. J. Mol. Recognit. 21, 267-274.
    • (2008) J. Mol. Recognit. , vol.21 , pp. 267-274
    • Zhang, Y.1    Tan, H.2    Jia, Z.3    Chen, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.