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Vol. 11, Issue 4, 1225-1239, April 2000
-Tubulin Alters Microtubule Dynamics and
Organization and Is Synthetically Lethal with the Kinesin-like Protein
Pkl1p
and
*Department of Molecular and Cell Biology, University of
California, Berkeley, California 94720-3200; Mitotic segregation of chromosomes requires spindle pole functions
for microtubule nucleation, minus end organization, and regulation of
dynamics. Department
of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210;
§Berkeley Electron Microscope Laboratory, University of
California, Berkeley, California 94720-3330; and Medical
Research Council Human Genetics Unit, Western General Hospital,
Edinburgh EH4 2XU, Scotland
-Tubulin is essential for nucleation, and we now extend
its role to these latter processes. We have characterized a mutation in
-tubulin that results in cold-sensitive mitotic arrest with an
elongated bipolar spindle but impaired anaphase A. At 30°C
cytoplasmic microtubule arrays are abnormal and bundle into single
larger arrays. Three-dimensional time-lapse video microscopy reveals
that microtubule dynamics are altered. Localization of the mutant
-tubulin is like the wild-type protein. Prediction of -tubulin
structure indicates that non-
/
-tubulin protein-protein
interactions could be affected. The kinesin-like protein (klp)
Pkl1p localizes to the spindle poles and spindle and is
essential for viability of the -tubulin mutant and in multicopy for
normal cell morphology at 30°C. Localization and function of Pkl1p in
the mutant appear unaltered, consistent with a redundant function for
this protein in wild type. Our data indicate a broader role for
-tubulin at spindle poles in regulating aspects of microtubule
dynamics and organization. We propose that Pkl1p rescues an impaired
function of -tubulin that involves non-tubulin protein-protein
interactions, presumably with a second motor, MAP, or MTOC component.
Online version of this article contains video
material for Figure 5. Online version available at www.molbiolcell.org.
Corresponding author. E-mail address:
jlpaluh{at}socrates.berkeley.edu.
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