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Calcium Inhibition of Physarum Myosin as Examined by the Recombinant Heavy Mero-Myosin

  • Hozumi Kawamichi
  • Ying Zhang
  • Mizuki Hino
  • Akio Nakamura
  • Hideyuki Tanaka
  • Lászlo Farkas
  • Lászlo Nyitray
  • Kazuhiro Kohama
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 592)

Abstract

Plasmodia of Physarum polycephalum shows vigorous cytoplasmic streaming by changing direction every few minutes. This oscillatory streaming is regulated by Ca2+ and is thought to be driven by a conventional myosin, i.e., by a myosin II isoform.1,2 While working as an assistant professor in Professor Ebashi’s laboratory at the University of Tokyo, one of the present authors (K.K.) induced the superprecipitation of actomyosin preparation or myosin B from the plasmodia to examine the effect of Ca2+. It superprecipitated without requiring Ca2+. When Ca2+ at μM level was present, the superprecipitation was inhibited.3 This calcium inhibition was quite the opposite of the superprecipitation of actomyosin from vertebrate muscles,4 and we expected that the inhibitory mode could be involved in the plant cytoplasmic streaming.2 With the finding of the diverse classes of unconventional myosin such as myosin I and V5 in vertebrate muscles, the inhibitory mode was shown to play a role in cell motility in both animal and plant kingdoms. In this case the myosins have calmodulin (CaM) as the light chains and are regulated by interaction of Ca2+ with CaM, which exerts an inhibitory effect on activity.5

Keywords

ATPase Activity Regulatory Light Chain Physarum Polycephalum Calcium Inhibition Essential Light Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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22.8. References

  1. 1.
    N. Kamiya, Physical and chemical basis of cytoplasmic streaming, Annu. Rev. Plant Physiol. 32, 205–236 (1981).CrossRefGoogle Scholar
  2. 2.
    A. Nakamura, K. Kohama, Calcium regulation of the actin-myosin interaction of Physarum polycephalum, Int. Rev. Cytol. 191, 53–98 (1999).PubMedCrossRefGoogle Scholar
  3. 3.
    K. Kohama, K. Kobayashi, and S. Mitani, Effects of Ca ion and ADP on superprecipitation of myosin B from slime mold, Physarum polycephalum, Proc. Jpn Acad. 56B, 591–596 (1980).Google Scholar
  4. 4.
    S. Ebashi and M. Endo, Calcium ion and muscle contraction, Prog. Biophys. Mol. Biol. 18, 123–183 (1968).PubMedCrossRefGoogle Scholar
  5. 5.
    J. S. Wolenski, Regulation of calmodulin-binding myosins, Trends Cell Biol. 5, 310–316 (1995).PubMedCrossRefGoogle Scholar
  6. 6.
    K. Kohama and J. Kendrick-Jones, The inhibitory Ca2+-regulation of the actin-activated Mg-ATPase activity of myosin from Physarum polycephalum plasmodia, J. Biochem. 99, 1433–1446 (1986).PubMedGoogle Scholar
  7. 7.
    R. Ishikawa, T. Okagaki, S. Higashi-Fujime, and K. Kohama, Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon, J. Biol. Chem. 266, 21784–21790 (1991).PubMedGoogle Scholar
  8. 8.
    K. Kohama, T. Okagaki, H. Takano-Ohmuro, and R. Ishikawa, Characterization of calcium-binding light chain as a Ca2+-receptive subunit of Physarum myosin, J. Biochem. 110, 566–570 (1991).PubMedGoogle Scholar
  9. 9.
    A. G. Szent-Gyorgyi, V. N. Kalabokis, and C. L. Perreault-Micale, Regulation by molluscan myosins, Mol. Cell. Biochem. 190, 55–62 (1999).PubMedCrossRefGoogle Scholar
  10. 10.
    S. Xie, D. H. Harrison, I. Schlichting, R. M. Sweet, V. N. Kalabokis, A. G. Szent-Gyorgyi, and C. Cohen, Structure of the regulatory domain of scallop myosin at 2.8 Å resolution, Nature 368, 306–312 (1994).PubMedCrossRefGoogle Scholar
  11. 11.
    T. Kobayashi, K. Tkagi, K. Konishi, Y. Hamada, M. Kawaguchi, and K. Kohama, Amino acid sequence of the calcium-binding light chain of myosin from the lower eukaryote, Physarum polycephalum, J. Biol. Chem. 263, 305–313 (1988).PubMedGoogle Scholar
  12. 12.
    L. Farkas, A. Malnasi-Csizmadia, A. Nakamura, K. Kohama, and L. Nyitray, Localization and characterization of the inhibitory Ca2+-binding site of Physarum polycephalum myosinII, J. Biol. Chem. 278, 27399–27405 (2003).PubMedCrossRefGoogle Scholar
  13. 13.
    K. Samizo, R. Ishikawa, A. Nakamura, and K. Kohama, A highly sensitive method for measurement of myosin ATPase activity by reversed-phase high-performance liquid chromatography, Anal. Biochem. 293, 212–215 (2001).PubMedCrossRefGoogle Scholar
  14. 14.
    A. Nakamura, Y. Hanyuda, T. Okagaki, and K. Kohama, A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephamum, Biochem. Biophys. Res. Commun. 328, 838–844 (2005).PubMedCrossRefGoogle Scholar

Copyright information

© Springer 2007

Authors and Affiliations

  • Hozumi Kawamichi
    • 1
    • 4
  • Ying Zhang
    • 1
  • Mizuki Hino
    • 1
  • Akio Nakamura
    • 1
  • Hideyuki Tanaka
    • 2
  • Lászlo Farkas
    • 3
  • Lászlo Nyitray
    • 3
  • Kazuhiro Kohama
    • 1
  1. 1.Department of Molecular and Cellular PharmacologyGunma University Graduate School of MedicineGunma
  2. 2.Department of Research SciencesGunma University School of Health ScienceMaebashi, Gunma
  3. 3.Department of BiochemistryEötvös-Loránd UniversityBudapestHungary
  4. 4.Department of Molecular PhysiologyYamaguchi University School of MedicineUbeJapan

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