Calcium inhibition of Physarum myosin as examined by the recombinant heavy mero-myosin.

作者: Hozumi Kawamichi , Ying Zhang , Mizuki Hino , Akio Nakamura , Hideyuki Tanaka

DOI: 10.1007/978-4-431-38453-3_22

关键词: CalmodulinCytoplasmic streamingPhysarumCell biologyMotilityChemistryPhysarum polycephalumMyosinCytoplasmMyosin light-chain kinase

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

参考文章(14)
T Kobayashi, T Takagi, K Konishi, Y Hamada, M Kawaguchi, K Kohama, Amino acid sequence of the calcium-binding light chain of myosin from the lower eukaryote, Physarum polycephalum. Journal of Biological Chemistry. ,vol. 263, pp. 305- 313 ,(1988) , 10.1016/S0021-9258(19)57393-8
S. Ebashi, M. Endo, Calcium ion and muscle contraction. Progress in Biophysics & Molecular Biology. ,vol. 18, pp. 123- 183 ,(1968) , 10.1016/0079-6107(68)90023-0
X. Xie, D. H. Harrison, I. Schlichting, R. M. Sweet, V. N. Kalabokis, A. G. Szent-Györgyi, C. Cohen, Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature. ,vol. 368, pp. 306- 312 ,(1994) , 10.1038/368306A0
Akio Nakamura, Kazuhiro Kohama, Calcium regulation of the actin-myosin interaction of Physarum polycephalum. International Review of Cytology-a Survey of Cell Biology. ,vol. 191, pp. 53- 98 ,(1999) , 10.1016/S0074-7696(08)60157-6
R. Ishikawa, T. Okagaki, S. Higashi-Fujime, K. Kohama, Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon. Journal of Biological Chemistry. ,vol. 266, pp. 21784- 21790 ,(1991) , 10.1016/S0021-9258(18)54705-0
Andrew G. Szent-Györgyi, Vassilios N. Kalabokis, Cynthia L. Perreault-Micale, Regulation by molluscan myosins. Molecular and Cellular Biochemistry. ,vol. 190, pp. 55- 62 ,(1999) , 10.1023/A:1006975705724
Kazuhiro KOHAMA, Keiko KOBAYASHI, Shohei MITANI, Effects of Ca Ion and ADP on Superprecipitation of Myosin B from Slime Mold, Physarum polycephalum Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences. ,vol. 56, pp. 591- 596 ,(1980) , 10.2183/PJAB.56.591
Akio Nakamura, Yuki Hanyuda, Tuyoshi Okagaki, Takashi Takagi, Kazuhiro Kohama, A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum. Biochemical and Biophysical Research Communications. ,vol. 328, pp. 838- 844 ,(2005) , 10.1016/J.BBRC.2005.01.035
Joseph S. Wolenski, Regulation of calmodulin-binding myosins Trends in Cell Biology. ,vol. 5, pp. 310- 316 ,(1995) , 10.1016/S0962-8924(00)89053-4