TY - JOUR
T1 - Interaction of monomeric and dimeric kinesin with microtubules
AU - Thormählen, M.
AU - Marx, A.
AU - Müller, S. A.
AU - Song, Y. H.
AU - Mandelkow, E. M.
AU - Aebi, U.
AU - Mandelkow, E.
N1 - Funding Information:
This work was supported by grants from the Deutsche Forschungsgemeinschaft (to E.M.M.), the Swiss National Science Foundation (grant 31-39691.93), the Canton Basel-Stadt, and the M.E. Müller Foundation of Switzerland.
Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1998/2/6
Y1 - 1998/2/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0039356659&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1997.1503
DO - 10.1006/jmbi.1997.1503
M3 - Journal articles
C2 - 9480770
AN - SCOPUS:0039356659
SN - 0022-2836
VL - 275
SP - 795
EP - 809
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 5
ER -
