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Plant and Cell Physiology Advance Access published online on October 4, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm126
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Binding of Chara Myosin Globular Tail Domain to Phospholipid Vesicles

Shun-ya Nunokawa, Hiromi Anan, Kiyo Shimada, You Hachikubo, Taku Kashiyama*, Kohji Ito and Keiichi Yamamoto§

Addresses: Department of Biology, Chiba University Yayoicho, Inage-ku, Chiba 263-8522, JAPAN
*Department of Pharmacology, Juntendo University, Medical School Hongo, Bunkyo-ku, Tokyo113-8500, JAPAN

§To whom all correspondence should be addressed: Prof. Keiichi Yamamoto, Address: Department of Biology, Chiba University Yayoicho, Inage-ku, Chiba 263-8522, JAPAN, Phone and fax: +81-43-290-2809, E-mail: yamamoto{at}bio.s.chiba-u.ac.jp


  Abstract

Binding of Chara myosin globular tail domain to phospholipid vesicles was investigated quantitatively. It was found that the globular tail domain binds to vesicles made from acidic phospholipids but not to those made from neutral phospholipids. This binding was weakened at high KCl concentration suggesting that the binding is electrostatic by nature. Dissociation constant for the binding of the globular tail domain to 20 % phosphatidyl serine vesicles (similar to endoplasmic reticulum in acidic phospholipid contents) at 150 mM KCl was 273 nM. Free energy change due to this binding calculated from the dissociation constant was -37.3 kJ mol-1. Thus the bond between the globular tail domain and membrane phospholipids would not be broken when the motor domain of Chara myosin moves along actin filament using energy of ATP hydrolysis ({triangleup}G°' = -30.5 kJ mol-1). Our results suggested that direct binding of Chara myosin to endoplasmic reticulum membrane through globular tail domain could work satisfactorily in Chara cytoplasmic streaming. We also suggested a possible regulatory mechanism of cytoplasmic streaming including phosphorylation-dependent dissociation of the globular tail domain from endoplasmic reticulum membrane.

Keywords: cytoplasmic streaming - plant myosin - globular tail domain - phospholipid binding - Ca2+ regulation - Chara corallina

(Received June 14, 2007; Revision received September 26, 2007. Accepted September 26, 2007)
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