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J Biol Chem, Vol. 274, Issue 16, 11339-11343, April 16, 1999
From the In the fission yeast Schizosaccharomyces
pombe, septation and constriction of the actomyosin ring for cell
division are positively regulated by the Spg1 GTPase, a member of the
Ras superfamily. Spg1 is negatively regulated by Byr4 and Cdc16, which
together form a two-component GTPase-activating protein for the Spg1
GTPase. To better understand how Byr4 regulates septation, Byr4 mutants were tested for in vitro functions. This analysis revealed
that Byr4 contained one Cdc16-binding site and four Spg1-binding sites (SBS), designated SBS1-SBS4. Although mutants with a single SBS bound
Spg1 and inhibited GTP dissociation, the equilibrium binding affinity
of these mutants was 28-280-fold weaker than Byr4. Because some Byr4
mutants with multiple SBSs bound Spg1 tighter than the corresponding
mutants with a single SBS, multiple SBSs probably interact to cause the
high affinity binding of Byr4 to Spg1. A region of Byr4 that bound
Spg1, SBS4, and the region that bound Cdc16, Cdc16-binding site, was
necessary and sufficient to form Cdc16-dependent Spg1GAP
activity that was similar to that of wild-type Byr4 with Cdc16.
Regions of Byr4, a Regulator of Septation in Fission Yeast, That
Bind Spg1 or Cdc16 and Form a Two-component GTPase-activating Protein
with Cdc16
,,
Department of Biochemistry, Vanderbilt
University School of Medicine, Nashville, Tennessee 37232 and the
¶ Department of Biochemistry, College of Science, Yonsei
University, Seoul 120-749, Korea
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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