Affordable Access

Publisher Website

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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Dynein arm substructure and the orientation of arm...

on Journal of Molecular Biology Mar 05, 1984

Substructure of the outer dynein arm.

on The Journal of Cell Biology December 1982

Substructure of the outer dynein arm

on The Journal of Cell Biology Jan 12, 1982

Microtubule binding and translocation by inner dyn...

on Cell Motility and the Cytoskel... 1991
More articles like this..