Binding of Chara myosin globular tail domain to phospholipid vesicles

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, su...

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Bibliographic Details
Published in:Plant and cell physiology 2007-11, Vol.48 (11), p.1558-1566
Main Authors: Nunokawa, S.(Chiba Univ. (Japan)), Anan, H, Shimada, K, Hachikubo, Y, Kashiyama, T, Ito, K, Yamamoto, K
Format: Article
Language:English
Subjects:
ALGAE
Ca2+ regulation
CALCIO
CALCIUM
Calcium - metabolism
Chara
Chara - metabolism
Chara corallina
CITOPLASMA
CYTOPLASM
CYTOPLASME
Cytoplasmic streaming
ENDOPLASMIC RETICULUM
FOSFOLIPIDOS
Globular tail domain
Kinetics
Liposomes - chemistry
Liposomes - metabolism
MEMBRANA
MEMBRANE
MEMBRANES
MIOSINA
MYOSIN
MYOSINE
Myosins - chemistry
Myosins - metabolism
PHOSPHATIDE
Phosphatidylinositols - chemistry
Phosphatidylinositols - metabolism
Phosphatidylserines - chemistry
Phosphatidylserines - metabolism
Phospholipid binding
PHOSPHOLIPIDS
Phospholipids - chemistry
Phospholipids - metabolism
Plant myosin
Potassium Chloride - pharmacology
Protein Binding - drug effects
Protein Structure, Tertiary
RETICULO ENDOPLASMATICO
RETICULUM ENDOPLASMIQUE
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Summary: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. The dissociation constant for the binding of the globular tail domain to 20% phosphatidylserine vesicles (similar to endoplasmic reticulum in acidic phospholipid contents) at 150 mM KCI was 273 nM. The free energy change due to this binding calculated from the dissociation constant was -37.3kJ/mol. Thus the bond between the globular tail domain and membrane phospholipids would not be broken when the motor domain of Chara myosin moves along the actin filament using the energy of ATP hydrolysis (deltaGsup(0)' = -30.5 kJ/mol). Our results suggested that direct binding of Chara myosin to the endoplasmic reticulum membrane through the globular tail domain could work satisfactorily in Chara cytoplasmic streaming. We also suggest a possible regulatory mechanism of cytoplasmic streaming including phosphorylation-dependent dissociation of the globular tail domain from the endoplasmic reticulum membrane.
ISSN:0032-0781
1471-9053
DOI:10.1093/pcp/pcm126