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J Biol Chem, Vol. 275, Issue 19, 14381-14387, May 12, 2000
From the Department of Biochemistry, Vanderbilt University School
of Medicine, Nashville, Tennessee 37232-0146
Cytokinesis and septation in the fission yeast
Schizosaccharomyces pombe are studied as a model for
mammalian cell division. In fission yeast, septation is positively
regulated by Spg1, a Ras family GTPase that localizes to spindle-pole
bodies (SPBs) throughout the cell cycle. As cells enter mitosis, Spg1
accumulates in an active, GTP-bound form and binds the Cdc7 protein
kinase to cause Cdc7 translocation to SPBs. Cdc7 disappears from one SPB in mid-anaphase and from the second SPB in late mitosis. Byr4 plus
Cdc16 negatively regulate septation by forming a two-component GTPase-activating protein for Spg1. These results led us to hypothesize that Byr4 localization to SPBs regulated the nucleotide state of Spg1,
due to its ability to form Spg1GAP activity with Cdc16 and thus the
binding of Cdc7 to Spg1 at SPBs. To test this hypothesis, Byr4
localization was determined using indirect immunofluorescence. This
analysis revealed that Byr4 was localized to SPBs that did not contain
Cdc7. In byr4
Byr4 Localizes to Spindle-Pole Bodies in a Cell Cycle-regulated
Manner to Control Cdc7 Localization and Septation in Fission Yeast*
,
mutants, Cdc7 localized to
interphase SPBs and only symmetrically localized to mitotic SPBs. In
contrast, Byr4 overexpression prevented Spg1 and Cdc7 localization to
SPBs. These results suggest that Byr4 localization to SPBs maintains
Spg1 in an inactive form, presumably by stimulating Spg1 GTPase
activity with Cdc16, and that loss of Byr4 from mitotic SPBs increases
the active fraction of Spg1 and thereby increases Spg1-Cdc7 binding.
Byr4 localization to SPBs was decreased in spg1,
cdc16, sid4, and cdc11 mutants as
well as in several mutants that affect medial F-actin structures, suggesting that multiple pathways regulate Byr4 localization to SPBs.
*
This work was supported in part by National Institutes of
Health (NIH) Grant GM51952 and Vanderbilt-Ingram Cancer Center Pilot Project Grant 99-11 (to C. A. from Cancer Center Support Grant 1P30
CA68485). Experiments were performed in part through the use of the
Vanderbilt University School of Medicine Cell Imaging Resource
(supported by NIH Grants CA68485 and DK20593).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported in part by a University Research Council Grant (to
C. A.).
§
Supported in part by NIH Grant T32-CA09582 (to G. Carpenter).
Present address: Van Andel Research Institute, 201 Monroe Ave. NW,
Suite 400, Grand Rapids, MI 49503.
¶
To whom correspondence should be addressed: DuPont
Pharmaceuticals, 500 S. Ridgeway Ave., Glenolden, PA 19036. Tel.:
610-237-7742; Fax: 610-237-7937; E-mail:
Charles.F.Albright@dupontpharma.com.
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