|
|
|
|
|
|
|
||
J. Cell Biol.,
Volume 141, Number 5, June 1, 1998 1169-1179
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853-2703
We have previously shown that Stu2p is a microtubule-binding protein and a component of the Saccharomyces cerevisiae spindle pole body (SPB). Here
we report the identification of Spc72p, a protein that interacts with Stu2p. Stu2p and Spc72p associate in the
two-hybrid system and can be coimmunoprecipitated
from yeast extracts. Stu2p and Spc72p also interact with
themselves, suggesting the possibility of a multimeric
Stu2p-Spc72p complex. Spc72p is an essential component of the SPB and is able to associate with a preexisting SPB, indicating that there is a dynamic exchange between soluble and SPB forms of Spc72p. Unlike
Stu2p, Spc72p does not bind microtubules in vitro, and
was not observed to localize along microtubules in vivo.
A temperature-sensitive spc72 mutation causes defects
in SPB morphology. In addition, most spc72 mutant cells lack cytoplasmic microtubules; the few cytoplasmic microtubules that are observed are excessively
long, and some of these are unattached to the SPB.
spc72 cells are able to duplicate and separate their
SPBs to form a bipolar spindle, but spindle elongation
and chromosome segregation rarely occur. The chromosome segregation block does not arrest the cell cycle; instead, spc72 cells undergo cytokinesis, producing
aploid cells and polyploid cells that contain multiple
SPBs.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
