An extended microtubule-binding structure within the dynein motor domain.
Gee, Melissa A.; Heuser, John E.; Vallee, Richard B.
[Letter]
Nature.
390(6660):636-639, December 11, 1997.
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Flagellar dynein was discovered over 30 years ago as the first motor protein capable of generating force along microtubules *RF 1*.A cytoplasmic form of dynein has also been identified which is involved in mitosis and a wide range of other intracellular movements [2] (reviewed in [3]). Rapid progress has been made on understanding the mechanism of force production by kinesis and myosins [4-8]. In contrast, progress in understanding the dyneins has been limited by their great size (relative molecular mass 1,000K-2,000K) and subunit complexity. We now report evidence that the entire carboxy-terminal two-thirds of the 532K force-producing heavy chain subunit is required for ATP-binding activity. We further identify a microtubule-binding domain, which, surprisingly, lies well downstream of the entire ATPase region and is predicted to form a hairpin-like stalk. Direct ultrastructural analysis of a recombinant fragment confirms this model, and suggests that the mechanisms for dynein force production differs substantially from that of other motor proteins.
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