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Dynein arm substructure and the orientation of arm-microtubule attachments

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
173
Issue
3
Identifiers
DOI: 10.1016/0022-2836(84)90127-x
Disciplines
  • Chemistry

Abstract

Abstract In the presence of AMP-PCP (β,γ-methyleneadenosine 5′-triphosphate), a non-hydrolyzable analog of ATP, negative stain images of increased morphological detail indicate that the dynein arm, attached to ciliary doublet microtubules, is composed of subunits including a cape, an elongated body and a head. The arrangement of these subunits makes it possible to distinguish A from B subfiber binding sites on a single arm and to demonstrate that the head of an extended arm on subfiber A of one ciliary doublet is capable of binding to subfiber B of an adjacent doublet in a specific orientation, which supports a key step in a current model of the mechanochemical cycle by which the arm produces microtubule sliding in the ciliary axoneme.

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