期刊
SCIENCE
卷 337, 期 6096, 页码 857-860出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1221698
关键词
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资金
- U.S. Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Robert A. Welch Foundation [I-1692]
- NIH [GM-098543]
Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use alpha beta-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of alpha beta-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast alpha beta-tubulin. TOG1 binds alpha beta-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of alpha beta-tubulin that cannot be incorporated into microtubules, contacting alpha- and beta-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with alpha beta-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of alpha beta-tubulin and how they selectively recognize the growing end of the microtubule.
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