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J. Biol. Chem., Vol. 277, Issue 42, 39585-39593, October 18, 2002
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From the SAM (sterile alpha
motif) domains are protein-protein interaction modules
found in a large number of regulatory proteins. Byr2 and Ste4 are two
SAM domain-containing proteins in the mating pheromone response pathway
of the fission yeast, Schizosaccharomyces pombe. Byr2 is a
mitogen-activated protein kinase kinase kinase that is regulated by
Ste4. Tu et al. (Tu, H., Barr, M., Dong, D. L., and
Wigler, M. (1997) Mol. Cell. Biol. 17, 5876-5887) showed that the isolated SAM domain of Byr2 binds a fragment of Ste4 that
contains both a leucine zipper (Ste4-LZ) domain as well as a SAM
domain, suggesting that Byr2-SAM and Ste4-SAM may form a hetero-oligomer. Here, we show that the individual SAM domains of Ste4
and Byr2 are monomeric at low concentrations and bind to each other in
a 1:1 stoichiometry with a relatively weak dissociation constant of
56 ± 3 µM. Inclusion of the Ste4-LZ domain, which determines the oligomeric state of Ste4, has a dramatic effect on
binding affinity, however. We find that the Ste4-LZ domain is trimeric
and, when included with the Ste4-SAM domain, yields a 3:1
Ste4-LZ-SAM:Byr2-SAM complex with a tight dissociation constant of
19 ± 4 nM. These results suggest that the Ste4-LZ-SAM
protein may recognize multiple binding sites on Byr2-SAM, indicating a new mode of oligomeric organization for SAM domains. The fact that high
affinity binding occurs only with the addition of an oligomerization
domain suggests that it may be necessary to include ancillary
oligomerization modules when searching for binding partners of SAM domains.
Oligomerization-dependent Association of the SAM
Domains from Schizosaccharomyces pombe Byr2 and Ste4*
§,§,,
,
Department of Chemistry and Biochemistry,
Molecular Biology Institute, and the UCLA-DOE Laboratory of
Structural Biology and Molecular Medicine, University of California,
Los Angeles, California 90095, the ¶ Departments of
Biochemistry and Chemistry and the Biotechnology Laboratory, University
of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada,
and Sunesis Pharmaceuticals,
San Francisco, California 94080
*
This work was supported by National Institutes of Health
Grant RO1CA81000 (to J. U. B.) and by the National Cancer
Institute of Canada with funds from the Canadian Cancer Society (to
L. P. M.).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.
Leukemia and Lymphoma Society Scholar. To whom correspondence
should be addressed: Boyer Hall, UCLA, 611 Charles E. Young Dr. E., Los
Angeles, CA 90095-1570. Tel.: 310-206-4747; Fax: 310-206-4749; E-mail: bowie@mbi.ucla.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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