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J Biol Chem, Vol. 273, Issue 15, 9285-9291, April 10, 1998
From the The major microtubule-associated protein in
echinoderms is a 77-kDa, WD repeat protein, called EMAP. EMAP-related
proteins have been identified in sea urchins, starfish, sanddollars,
and humans. We describe the purification of sea urchin EMAP and
demonstrate that EMAP binding to microtubules is saturable at a molar
ratio of 1 mol of EMAP to 3 mol of tubulin dimer. Unlike MAP-2, MAP-4, or tau proteins, EMAP binding to microtubules is not lost by cleavage of tubulin with subtilisin. In addition to binding to the microtubule polymer, EMAP binds to tubulin dimers in a 1:1 molar ratio. The abundance of EMAP in the egg suggests that it could function to regulate microtubule assembly. To test this hypothesis, we examined the
effects of EMAP on the dynamic instability of microtubules nucleated
from axoneme fragments as monitored by video-enhanced differential
interference contrast microscopy. Addition of 2.2 µM EMAP to 21 µM tubulin results in a
slight increase in the elongation and shortening velocities at the
microtubule plus ends but not at the minus ends. Significantly, EMAP
inhibits the frequency of rescue 8-fold without producing a change in
the frequency of catastrophe. These results indicate that EMAP, unlike
brain microtubule-associated proteins, promotes microtubule
dynamics.
Purification of a WD Repeat Protein, EMAP, That Promotes
Microtubule Dynamics through an Inhibition of Rescue
,
Department of Biochemistry, Cell and
Molecular Biology, University of Kansas, Lawrence, Kansas 66045 and the § Department of Biological Sciences, Lehigh
University, Bethlehem, Pennsylvania 18015
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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