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Plant and Cell Physiology, 2001, Vol. 42, No. 8 828-834
© 2001 Oxford University Press

Effects of Ca2+ and Calmodulin on the Motile Activity of Characean Myosin In vitro

Jun-ya Awata, Kazuhiro Saitoh, Kiyo Shimada, Taku Kashiyama and Keiichi Yamamoto1

Department of Biology, Faculty of Science, Chiba University, Yayoi-cho, Inage-ku, Chiba 263-8522 Japan

It is well known that the cytoplasmic streaming of characean cells is readily inhibited by Ca2+. However, neither the actin-activated MgATPase nor the in vitro motile activity of purified characean myosin were inhibited by Ca2+. Recently, amino acid sequence of characean myosin was determined in our laboratory and the sequence revealed that characean myosin contains six calmodulin binding sites in the neck region. We also detected calmodulin in quickly prepared characean myosin fraction. It is, therefore, possible that the insensitivity of characean myosin to Ca2+ is due to the dissociation of some calmodulin molecules from the neck region during the course of protein purification. To determine strictly the Ca2+ sensitivity of characean myosin, we intentionally used crude preparation of characean myosin to reduce the possibility of calmodulin dissociation and examined the motile activity of characean myosin in vitro in the presence of excess characean calmodulin. We could not observe any drastic inhibition of characean myosin activity by Ca2+. The results suggest that the brief cessation of cytoplamic streaming is not caused by the direct inhibition of myosin activity by Ca2+.

1 Corresponding author: E-mail, yamamoto@bio.s.chiba-u.ac.jp; Fax, +81-43-290-2809.


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