A one-headed class V myosin molecule develops multiple large ( 32-nm) steps successively
نویسندگان
چکیده
منابع مشابه
A one - headed class V myosin molecule develops multiple large ( 32 - nm ) steps successively
*Formation of Soft Nanomachines, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, †Single Molecule Processes Project, International Cooperative Research Project, Japan Science and Technology Agency, ‡Department of Biophysical Engineering, Osaka University, §Soft Biosystem Group, Laboratories for Nanobiology, Graduate School of Frontier Biosciences, Osak...
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Class V myosin (myosin-V) is a cargo transporter that moves along an actin filament with large (approximately 36-nm) successive steps. It consists of two heads that each includes a motor domain and a long (23 nm) neck domain. One of the more popular models describing these steps, the hand-over-hand model, assumes the two-headed structure is imperative. However, we previously succeeded in observ...
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Chicken myosin-V is a member of a recently recognized class of myosins distinct from both the myosins-I and the myosins-II. We report here the purification, electron microscopic visualization, and motor properties of a protein of this class. Myosin-V molecules consist of two heads attached to an approximately 30 nm stalk that ends in a globular region of unknown function. Myosin-V binds to and ...
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Myosin V is a two-headed molecular motor that binds six light chains per heavy chain, which creates unusually long lever arms. This motor moves processively along its actin track in discrete 36-nm steps. Our model is that one head of the two-headed myosin V tightly binds to actin and swings its long lever arm through a large angle, providing a stroke. We created single-headed constructs with di...
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It is widely accepted that the vesicle-transporter myosin-V moves processively along F-actin with large steps of approximately 36 nm using a hand-over-hand mechanism. A key question is how does the rear head of two-headed myosin-V search for the forward actin target in the forward direction. Scanning probe nanometry was used to resolve this underlying search process, which was made possible by ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2004
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0402914101