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Vol. 8, Issue 12, 2575-2590, December 1997
Department of Biochemistry, University of Washington, Seattle,
Washington 98195-7350
The central coiled coil of the essential spindle pole component
Spc110p spans the distance between the central and inner plaques of the
Saccharomyces cerevisiae spindle pole body (SPB). The
carboxy terminus of Spc110p, which binds calmodulin, resides at the
central plaque, and the amino terminus resides at the inner plaque from which nuclear microtubules originate. To dissect the functions of
Spc110p, we created temperature-sensitive mutations in the amino and
carboxy termini. Analysis of the temperature-sensitive spc110 mutations and intragenic complementation analysis
of the spc110 alleles defined three functional regions
of Spc110p. Region I is located at the amino terminus. Region II is
located at the carboxy-terminal end of the coiled coil, and region III
is the previously defined calmodulin-binding site. Overexpression of SPC98 suppresses the temperature sensitivity conferred
by mutations in region I but not the phenotypes conferred by mutations
in the other two regions, suggesting that the amino terminus of Spc110p is involved in an interaction with the 
-tubulin complex composed of
Spc97p, Spc98p, and Tub4p. Mutations in region II lead to loss of SPB
integrity during mitosis, suggesting that this region is required for
the stable attachment of Spc110p to the central plaque. Our results
strongly argue that Spc110p links the -tubulin complex to the
central plaque of the SPB.
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