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Vol. 9, Issue 7, 1741-1756, July 1998
and
*Department of Cancer Biology, Dana-Farber Cancer Institute, and
Department of Biological Chemistry and Molecular Pharmacology, Harvard
Medical School, Boston, Massachusetts 02115; and
Although vertebrate cytoplasmic dynein can move to the minus ends
of microtubules in vitro, its ability to translocate purified vesicles
on microtubules depends on the presence of an accessory complex known
as dynactin. We have cloned and characterized a novel gene,
NIP100, which encodes the yeast homologue of the
vertebrate dynactin complex protein p150glued. Like strains
lacking the cytoplasmic dynein heavy chain Dyn1p or the centractin
homologue Act5p, nip100Department of Biology, The Johns Hopkins University,
Baltimore, Maryland 21218
strains are viable but
undergo a significant number of failed mitoses in which the mitotic
spindle does not properly partition into the daughter cell. Analysis of
spindle dynamics by time-lapse digital microscopy indicates that the
precise role of Nip100p during anaphase is to promote the translocation
of the partially elongated mitotic spindle through the bud neck.
Consistent with the presence of a true dynactin complex in yeast,
Nip100p exists in a stable complex with Act5p as well as Jnm1p, another
protein required for proper spindle partitioning during anaphase.
Moreover, genetic depletion experiments indicate that the binding of
Nip100p to Act5p is dependent on the presence of Jnm1p. Finally, we
find that a fusion of Nip100p to the green fluorescent protein
localizes to the spindle poles throughout the cell cycle. Taken
together, these results suggest that the yeast dynactin complex and
cytoplasmic dynein together define a physiological pathway that is
responsible for spindle translocation late in anaphase.
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