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Vol. 9, Issue 4, 759-774, April 1998
Department of Molecular, Cellular, and Developmental Biology,
University of Colorado, Boulder, Colorado 80309-0347
In Saccharomyces cerevisiae, the Mps1p protein
kinase is critical for both spindle pole body (SPB) duplication and the
mitotic spindle assembly checkpoint. The mps1-1
mutation causes failure early in SPB duplication, and because the
spindle assembly checkpoint is also compromised, mps1-1
cells proceed with a monopolar mitosis and rapidly lose viability. Here
we report the genetic and molecular characterization of
mps1-1 and five new temperature-sensitive alleles of
MPS1. Each of the six alleles contains a single point mutation in the region of the gene encoding the protein kinase domain.
The mutations affect several residues conserved among protein kinases,
most notably the invariant glutamate in subdomain III. In vivo and in
vitro kinase activity of the six epitope-tagged mutant proteins varies
widely. Only two display appreciable in vitro activity, and
interestingly, this activity is not thermolabile under the assay
conditions used. While five of the six alleles cause SPB duplication to
fail early, yielding cells with a single SPB, mps1-737
cells proceed into SPB duplication and assemble a second SPB that is
structurally defective. This phenotype, together with the observation
of intragenic complementation between this unique allele and two
others, suggests that Mps1p is required for multiple events in SPB
duplication.
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