Dynein arm substructure and the orientation of arm-microtubule attachments

Jock Avolio, Stephen Lebduska, Peter Satir

Research output: Contribution to journalArticle

24 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)389-401
Number of pages13
JournalJournal of Molecular Biology
Volume173
Issue number3
DOIs
StatePublished - Mar 5 1984

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Dyneins
Microtubules
Arm
Head
Axoneme
Coloring Agents
Adenosine Triphosphate
Binding Sites

ASJC Scopus subject areas

  • Virology

Cite this

Dynein arm substructure and the orientation of arm-microtubule attachments. / Avolio, Jock; Lebduska, Stephen; Satir, Peter.

In: Journal of Molecular Biology, Vol. 173, No. 3, 05.03.1984, p. 389-401.

Research output: Contribution to journalArticle

Avolio, Jock ; Lebduska, Stephen ; Satir, Peter. / Dynein arm substructure and the orientation of arm-microtubule attachments. In: Journal of Molecular Biology. 1984 ; Vol. 173, No. 3. pp. 389-401.
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