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-Tubulin Mutant Destabilizes the Heterodimer: Phenotypic
Consequences and Interactions with Tubulin-binding Proteins
Department of Biology and Center for Cancer Research, Massachusetts
Institute of Technology, Cambridge, Massachusetts 02139
Many effectors of microtubule assembly in vitro enhance the
polymerization of subunits. However, several Saccharomyces
cerevisiae genes that affect cellular microtubule-dependent
processes appear to act at other steps in assembly and to affect
polymerization only indirectly. Here we use a mutant 
-tubulin to
probe cellular regulation of microtubule assembly.
tub1-724 mutant cells arrest at low temperature with no
assembled microtubules. The results of several assays reported here
demonstrate that the heterodimer formed between Tub1-724p and
-tubulin is less stable than wild-type heterodimer. The unstable
heterodimer explains several conditional phenotypes conferred by the
mutation. These include the lethality of tub1-724
haploid cells when the -tubulin-binding protein Rbl2p is either
overexpressed or absent. It also explains why the
TUB1/tub1-724 heterozygotes are cold sensitive for
growth and why overexpression of Rbl2p rescues that conditional
lethality. Both haploid and heterozygous tub1-724 cells
are inviable when another microtubule effector, PAC2, is
overexpressed. These effects are explained by the ability of Pac2p to
bind -tubulin, a complex we demonstrate directly. The results
suggest that tubulin-binding proteins can participate in equilibria
between the heterodimer and its components.
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