Abstract
We have expressed the recombinant squid kinesin head domain in Escherichia coli and studied its interaction with microtubules. The head is active as a microtubule-stimulated ATPase and binds to microtubules, but it does not support microtubule gliding by itself. The head binds to both microtubules and depolymerized tubulin. In each case the zero-length crosslinker 1-ethyl-3-[3-dimethylamino)propyl] carbodiimide induces a bond specifically to beta- but not alpha-tubulin. The head decorates brain microtubules with an 8-nm axial spacing. Thus the stoichiometry is one kinesin head per tubulin dimer. The lattice is that of flagellar B-tubules, implying that reassembled microtubules are not symmetric. Moreover, the A- and B-tubules of intact flagellar outer doublets are both decorated with a B lattice. This suggests that the B lattice is a general property of microtubules.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 8:40 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 1:32 p.m.) |
Indexed | 1 month, 4 weeks ago (July 2, 2025, 2:46 p.m.) |
Issued | 32 years, 6 months ago (March 1, 1993) |
Published | 32 years, 6 months ago (March 1, 1993) |
Published Online | 32 years, 6 months ago (March 1, 1993) |
Published Print | 32 years, 6 months ago (March 1, 1993) |
@article{Song_1993, title={Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice.}, volume={90}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.90.5.1671}, DOI={10.1073/pnas.90.5.1671}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Song, Y H and Mandelkow, E}, year={1993}, month=mar, pages={1671–1675} }