An extended microtubule-binding structure within the dynein motor domain

Melissa A. Gee, John E. Heuser and Richard B. Vallee ()
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Melissa A. Gee: Worcester Foundation for Biomedical Research
John E. Heuser: Washington University
Richard B. Vallee: Worcester Foundation for Biomedical Research

Nature, 1997, vol. 390, issue 6660, 636-639

Abstract: Abstract Flagellar dynein was discovered over 30 years ago as the first motor protein capable of generating force along microtubules1. A cytoplasmic form of dynein has also been identified which is involved in mitosis and a wide range of other intracellular movements2 (reviewed in ref. 3). Rapid progress has been made on understanding the mechanism of force production by kinesins and myosins4,5,6,7,8. 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 mechanism for dynein force production differs substantially from that of other motor proteins.

Date: 1997
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DOI: 10.1038/37663

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