AAA+ Ring and Linker Swing Mechanism in the Dynein Motor
نویسندگان
چکیده
منابع مشابه
AAA+ Ring and Linker Swing Mechanism in the Dynein Motor
Dynein ATPases power diverse microtubule-based motilities. Each dynein motor domain comprises a ring-like head containing six AAA+ modules and N- and C-terminal regions, together with a stalk that binds microtubules. How these subdomains are arranged and generate force remains poorly understood. Here, using electron microscopy and image processing of tagged and truncated Dictyostelium cytoplasm...
متن کاملMolecular mechanism of force generation by dynein, a molecular motor belonging to the AAA+ family.
Dynein is an AAA+ (ATPase associated with various cellular activities)-type motor complex that utilizes ATP hydrolysis to actively drive microtubule sliding. The dynein heavy chain (molecular mass >500 kDa) contains six tandemly linked AAA+ modules and exhibits full motor activities. Detailed molecular dissection of this motor with unique architecture was hampered by the lack of an expression s...
متن کاملA structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein
Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusu...
متن کاملATP-Driven Remodeling of the Linker Domain in the Dynein Motor
Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar...
متن کاملReview: Structure and mechanism of the dynein motor ATPase
Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C-terminal 3500 amino-acid residues form the motor domain, which hydrolyses ATP in its ring of AAA+ (ATPases associated with diverse cellular activities) domains to generate the force for movement. The production of forc...
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ژورنال
عنوان ژورنال: Cell
سال: 2009
ISSN: 0092-8674
DOI: 10.1016/j.cell.2008.11.049