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PMID: 16466743 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

A flexible linkage between the dynein motor and its cargo.

Journal of molecular biology ·Vol. 357 ·No. 3 ·2006-03-31 ·Pages 701-6

Meng X, Samsó M, Koonce MP

Abstract

We have used an antibody-Fab tag to mark the position of the cytoplasmic dynein amino-terminal tail domain, as it emerges from the main mass of the motor. Electron microscopy and single-particle image analysis reveal that the tag does not assume a rigidly fixed position, but instead can be found at various locations around the planar ring that comprises the motor's backbone. The work suggests that the tail is attached to the motor at a point near the ring center, and that the sequence immediately adjacent to this connection is flexible. Such flexibility argues against a simple-lever arm model for dynein force production.

MeSH Terms
Animals Dictyostelium/enzymology Dyneins/chemistry,metabolism,ultrastructure Models, Molecular Molecular Motor Proteins/chemistry,metabolism,ultrastructure
Chemicals
Molecular Motor Proteins Dyneins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Meng Xing
Division of Molecular Medicine, Wadsworth Center, Albany, NY 12201, USA.
Samsó Montserrat
Koonce Michael P
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
2006-03-31
Epub
2006-00-26
Pages
701-6
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NCRR NIH HHS · 2P41RR01219 · United States
NIGMS NIH HHS · GM51532 · United States
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