The Dynein Stalk Contains an Antiparallel Coiled Coil with Region-Specific Stability

The dynein motor proteins interact with microtubules at the distal end of an unusual 12−15 nm stalk, which communicates with the sites for nucleotide hydrolysis and microtubule binding in a cyclical, bidirectional manner. Here, we report that the stalk shaft of rat cytoplasmic dynein is an antiparal...

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Bibliographic Details
Published in:Biochemistry (Easton) 2009-03, Vol.48 (12), p.2710-2713
Main Authors: Höök, Peter, Yagi, Toshiki, Ghosh-Roy, Anindya, Williams, John C, Vallee, Richard B
Format: Article
Language:English
Subjects:
Animals
Dyneins - chemistry
Dyneins - metabolism
Microtubule-Associated Proteins - chemistry
Microtubule-Associated Proteins - metabolism
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation
Rats
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Summary:The dynein motor proteins interact with microtubules at the distal end of an unusual 12−15 nm stalk, which communicates with the sites for nucleotide hydrolysis and microtubule binding in a cyclical, bidirectional manner. Here, we report that the stalk shaft of rat cytoplasmic dynein is an antiparallel α-helical coiled coil, the stability of which is markedly altered by changes at its proximal and distal ends, consistent with a structure capable of rapid, cyclical rearrangement during the dynein cross-bridge cycle.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi900223x