A flexible linkage between the dynein motor and its cargo

J Mol Biol. 2006 Mar 31;357(3):701-6. doi: 10.1016/j.jmb.2006.01.028. Epub 2006 Jan 26.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Dictyostelium / enzymology
  • Dyneins / chemistry*
  • Dyneins / metabolism*
  • Dyneins / ultrastructure
  • Models, Molecular
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / metabolism*
  • Molecular Motor Proteins / ultrastructure

Substances

  • Molecular Motor Proteins
  • Dyneins