An extended microtubule-binding structure within the dynein motor domain

Flagellar dynein was discovered over 30 years ago as the first motor protein capable of generating force along microtubules. A cytoplasmic form of dynein has also been identified which is involved in mitosis and a wide range of other intracellular movements (reviewed in ref. 3). Rapid progress has b...

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Bibliographic Details
Published inNature (London) Vol. 390; no. 6660; pp. 636 - 639
Main Authors Vallee, Richard B, Gee, Melissa A, Heuser, John E
Format Journal Article
LanguageEnglish
Published London Nature Publishing 11.12.1997
Nature Publishing Group
Subjects
Analytical, structural and metabolic biochemistry
Animals
ATP
Binding Sites
Biological and medical sciences
Cell division
Cloning, Molecular
Contractile proteins
COS Cells
Dyneins - chemistry
Dyneins - genetics
Dyneins - metabolism
Dyneins - ultrastructure
Fundamental and applied biological sciences. Psychology
Genes
Holoproteins
Microtubules - metabolism
Mutation
Proteins
Rats
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Vertebrata
Mammalia
Rat
Structure activity relation
Enzyme
Rodentia
Contractile protein
Hydrolases
Binding site
Dynein ATPase
Microtubule
Biological activity
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Summary:Flagellar dynein was discovered over 30 years ago as the first motor protein capable of generating force along microtubules. A cytoplasmic form of dynein has also been identified which is involved in mitosis and a wide range of other intracellular movements (reviewed in ref. 3). Rapid progress has been made on understanding the mechanism of force production by kinesins and myosins. 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.
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ISSN:0028-0836
1476-4687
DOI:10.1038/37663