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J. Biol. Chem., Vol. 268, Issue 5, 3414-3419, Feb, 1993
R Brandt and G Lee
Tau protein is a microtubule-associated protein that is almost exclusively
expressed in the brain and is enriched in the axon. Determination of tau's
sequence has revealed three to four tandem repeats that have been shown to
constitute the microtubule binding site. In order to study the functional
organization of tau, we prepared a series of truncated tau fragments using
an Escherichia coli expression system. We assayed each fragment's activity
in promoting growth of microtubules and in nucleating free microtubules. We
found that tau's ability to nucleate microtubules requires the presence of
additional sequence amino-terminal to that required for growth. We
demonstrate that tau's carboxyl and amino termini differentially affect
microtubule growth and nucleation. Finally, we show that in vitro
microtubule bundle formation occurs when tubulin is assembled in the
presence of an amino- and carboxyl-terminally truncated tau protein,
whereas almost no bundling is observed in the presence of full-length tau
or tau fragments that contain the amino terminus in addition to the repeat
domain. We conclude that although the presence of the repeat domain
promotes the growth of microtubules, the structural requirements for
nucleation activity are more stringent. The differentiation between the
growth promoting and nucleation activities on the structural level makes it
possible for the two activities to be differentially regulated in vivo.
Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro
Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115.
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