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Vol. 11, Issue 5, 1887-1903, May 2000
§
*Department of Genetics, Stanford University School of Medicine,
Stanford, California 94305; A comprehensive set of clustered charged-to-alanine mutations was
generated that systematically alter TUB1, the major
Department of Molecular and
Cell Biology, University of California at Berkeley, Berkeley,
California 94720; and §Lawrence Berkeley National
Laboratory, Berkeley, California 94720
-tubulin gene of Saccharomyces cerevisiae. A variety
of phenotypes were observed, including supersensitivity and resistance
to the microtubule-destabilizing drug benomyl, lethality, and cold- and
temperature-sensitive lethality. Many of the most benomyl-sensitive
tub1 alleles were synthetically lethal in combination
with tub3
, supporting the idea that benomyl supersensitivity is a rough measure of microtubule instability and/or
insufficiency in the amount of -tubulin. The systematic tub1 mutations were placed, along with the comparable
set of tub2 mutations previously described, onto
a model of the yeast -
-tubulin dimer based on the
three-dimensional structure of bovine tubulin. The modeling revealed a
potential site for binding of benomyl in the core of -tubulin.
Residues whose mutation causes cold sensitivity were concentrated at
the lateral and longitudinal interfaces between adjacent subunits.
Residues that affect binding of the microtubule-binding protein Bim1p
form a large patch across the exterior-facing surface of -tubulin in
the model. Finally, the positions of the mutations suggest that
proximity to the - interface may account for the finding of
synthetic lethality of five viable tub1 alleles with the
benomyl-resistant but otherwise entirely viable tub2-201 allele.
A complete data set for this article is available at
www.molbiolcell.org.
These authors contributed equally to this work.
Corresponding author. E-mail
address: botstein{at}genome.stanford.edu.
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