Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice.

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.

authors

Song YH,Mandelkow E

doi

10.1073/pnas.90.5.1671

subject

Has Abstract

pub_date

1993-03-01 00:00:00

pages

1671-5

issue

5

eissn

0027-8424

issn

1091-6490

journal_volume

90

pub_type

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