Interaction Between Calmodulin and Target Proteins (original) (raw)

Abstract

When myosin light chain kinase (MLCK) activity was measured at various different free Ca2+ concentrations, the activity attained abruptively the maximum value within a very narrow concentration range of Ca2+. A result of this phenomenon is shown in Fig.1 (curve e), accompanied with the Ca2+ binding curve of calmodulin (curve a) (1). Since the Ca2+-calmodulin is known to work as an activator of MLCK, a large difference between the enzyme activation curve and the Ca2+ binding curve of calmodulin indicates that Ca2+ effect on the MLCK activity can not directly be explained by the comparison of these two curves. Olwin et al. have already shown that the affinity of Ca2+ to calmodulin was largely enhanced by the addition of MLCK (2). It is expected that the analysis of enhancing effect of MLCK to-the Ca2+ binding to calmodulin may give an answer how the enzyme attains the maximum activity within such a narrow concentration range of Ca2+ and how the Ca2+ concentration is fixed to this range. The Ca2+ binding to calmodulin was measured in the presence of mastoparan (curve c in Fig. 1) (3). Mastoparan is a small peptide composed of 14 amino acid residues, and Malencik and Anderson have reported a strong binding constant of mastoparan to calmodulin (4).

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References

  1. O. Minowa and K. Yagi, Calcium binding to tryptic fragments of calmodulin, J. Biochem. 96:1175 (1984)
    PubMed CAS Google Scholar
  2. B.B. Olwin, A.M. Edelman, E.G. Krebs, and D.R. Storm, Quantitation of energy coupling between Ca2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates, J. Biol. Chem. 259:10949 (1984)
    PubMed CAS Google Scholar
  3. M. Yazawa, M. Ikura, K. Hikichi, Y. Luan and K. Yagi, Communication between two globular domains of calmodlulin in the presence of mastoparan or caldesmon fragment. Ca2+ binding and 1H NMR, J. Biol. Chem. 262:10951 (1987)
    PubMed CAS Google Scholar
  4. D.A. Malencik and S.R. Anderson, High affinity binding of the mastoparans by calmodulin, Biochem. Biophys. Res. Commun. 114:50 (1983)
    Article PubMed CAS Google Scholar
  5. Y.S. Babu, J.S. Sack, T.J. Greenhough, C.E. Bugg, A.R. Means and W.J. Cook, Three-dimensional structure of calmoldulin, Nature 315:37 (1985)
    Article PubMed CAS Google Scholar
  6. W. Drabikowski, H. Brzeska and S.Y. Venyaminov, Tryptic fragments of calmodulin. Ca2+ - and Mg2+-induced conformational changes, J. Biol. Chem. 257:11584 (1982)
    PubMed CAS Google Scholar
  7. M. Ikura., T. Hiraoki, K. Hikichi, O. Minowa, H. Yamaguchi, M. Yazawa and K. Yagi, Nuclear magnetic resonance studies on calmodulin: Ca2+-dependent spectral change of proteolytic fragments, Biochemistry 23:3124 (1984)
    Article CAS Google Scholar
  8. M. Ikura, O. Minowa, M. Yazawa, K. Yagi and K. Hikichi, Sequence-specific assignments of downfield-shifted amide proton resonances of calmodulin, FEBS Lett. 219:17 (1987)
    Article CAS Google Scholar
  9. M. Yazawa, E. Kawamura, O. Minowa, K. Yagi, M. Ikura and K. Hikichi, N-terminal region (Domain 1) of calmodulin is the low affinity site for Ca2+. A 13C NMR study of S-cyanocalmodulin, J. Biochem. 95:443 (1984)
    PubMed CAS Google Scholar
  10. D.K. Blumenthal, K. Takio, A.M. Edelman, H. Charbonneau, K. Titani, K.A. Walsh and E.G. Krebs, Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase, Proc. Natl. Acad. Sci. USA 82:3187 (1985)
    Article PubMed CAS Google Scholar
  11. M. Ikura, N. Hasegawa, K. Hikichi, S. Aimoto, M. Yazawa and K. Yagi, 113Cd-NMR Evidence for cooperative interaction between the amino-and carboxyl-terminal domains of calmodulin, in preparation
    Google Scholar
  12. S. Forsen, E. Thulin, T. Drakenberg, J. Krebs and K. Seamon, A 113Cd NMR study of calmodulin and its interaction with calcium, magnesium and trifluoperazine, FEBS Lett. 117:189 (1980)
    Article PubMed CAS Google Scholar

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Authors and Affiliations

  1. Department of Chemistry and High Resolution, Faculty of Science, Hokkaido University, Sapporo 060, Japan
    Koichi Yagi & Michio Yazawa
  2. NMR Laboratory, Faculty of Science, Hokkaido University, Sapporo 060, Japan
    Mitsuhiko Ikura & Kunio Hikichi

Authors

  1. Koichi Yagi
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  2. Michio Yazawa
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  3. Mitsuhiko Ikura
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  4. Kunio Hikichi
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Editor information

Editors and Affiliations

  1. Nagoya University, Nagoya, Japan
    H. Hidaka
  2. Swiss Federal Institute of Technology, Zurich, Switzerland
    E. Carafoli
  3. Baylor College of Medicine, Houston, Texas, USA
    A. R. Means
  4. Mie University School of Medicine, Mie, Japan
    T. Tanaka

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© 1989 Plenum Press, New York

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Yagi, K., Yazawa, M., Ikura, M., Hikichi, K. (1989). Interaction Between Calmodulin and Target Proteins. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0\_16

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