Interaction of monomeric and dimeric kinesin with microtubules.

Abstract:

:The binding stoichiometry of kinesin to microtubules was determined using several biochemical and biophysical approaches (chemical crosslinking, binding assays, scanning transmission electron microscopy (STEM), image reconstruction, and X-ray scattering). The results show that each tubulin dimer associates with one kinesin head, irrespective of whether kinesin occurs in a monomeric or dimeric form in solution. Moreover, these heads appear to align along the protofilament axis generating a 16 nm periodicity of successive kinesin dimers. This is consistent with a "tightrope" model of movement where the first head of the dimer provides a guiding signal for the following one.

journal_name

J Mol Biol

authors

Thormählen M,Marx A,Müller SA,Song Y,Mandelkow EM,Aebi U,Mandelkow E

doi

10.1006/jmbi.1997.1503

subject

Has Abstract

pub_date

1998-02-06 00:00:00

pages

795-809

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022283697915035

journal_volume

275

pub_type

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