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J. Biol. Chem., Vol. 265, Issue 3, 1794-1799, 01, 1990
A Banerjee, MC Roach, P Trcka and RF Luduena
Tubulin, the major constituent protein of microtubules, is a heterodimer of
alpha and beta subunits. Both alpha and beta exist in multiple isotypic
forms. It is not clear if different isotypes perform different functions.
In order to approach this question, we have made a monoclonal antibody
specific for the beta III isotype of tubulin. This particular isotype is
neuron-specific and appears to be phosphorylated near the C terminus. We
have used immunoaffinity depletion chromatography to prepare tubulin
lacking the beta III subunit. We find that removal of the beta III isotype
results in a tubulin mixture able to assemble much more rapidly than is
unfractionated tubulin when reconstituted with either of the two
microtubule-associated proteins (MAPs), tau or MAP 2. Our results suggest
that the different isotypes of tubulin differ from each other in their
ability to polymerize into microtubules. We have also found that the
anti-beta III antibody can stimulate microtubule assembly when
reconstituted with tubulin and either tau or MAP 2. When reconstituted with
tubulin lacking the beta III isotype, the antibody causes the tubulin to
polymerize into a polymer that is a microtubule in the presence of MAP 2
and a ribbon in the presence of tau.
Increased microtubule assembly in bovine brain tubulin lacking the type III isotype of beta-tubulin
Department of Biochemistry, University of Texas Health Science Center, San Antonio 78284.
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