Abstract
THE 'motor' proteins of eukaryotic cells contain specialized domains that hydrolyse ATP to produce force and movement along a cytoskeletal polymer (actin in the case of the myosin family; microtubules in the case of the kinesin family and dyneins). There are motor-protein superfamilies in which each member has a conserved force-generating domain joined to a different 'tail' which conveys specific attachment properties (see ref. 1 for a review). The minus-end-directed microtubule motors, the dyneins2, may also constitute a superfamily of force-generating proteins with distinct attachment domains3. Axonemal outer-arm dynein from sea urchin spermatozoa is a multimeric protein consisting of two heavy chains (α and β) with ATPase activity, three intermediate chains and several light chains4. Here I report the sequence of cloned complementary DNA encoding the β heavy chain of a dynein motor molecule. The predicted amino-acid sequence reveals four ATP-binding consensus sequences in the central domain. The dynein β heavy chain is thought to associate transiently with a microtubule during ATP hydrolysis5, but the ATP-dependent microtubule-binding sequence common to the kinesin superfamily is not found in the dynein β heavy chain. These unique features distinguish the dynein β heavy chain from other motor protein superfamilies and may be characteristic of the dynein superfamily.
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Ogawa, K. Four ATP-binding sites in the midregion of the β heavy chain of dynein. Nature 352, 643–645 (1991). https://doi.org/10.1038/352643a0
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DOI: https://doi.org/10.1038/352643a0
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