A TOG:αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.
A TOG:αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.
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DOI:
10.1126/science.1221698
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发表时间:
2012-08-17
期刊:
影响因子:
--
通讯作者:
Rice LM
中科院分区:
文献类型:
--
作者:
Ayaz P;Ye X;Huddleston P;Brautigam CA;Rice LM
Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use αβ-tubulin–interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of αβ-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 αβ-tubulin. TOG1 binds αβ-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of αβ-tubulin that cannot be incorporated into microtubules, contacting α- and β-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with αβ-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin and how they selectively recognize the growing end of the microtubule.
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DOI:
10.1073/pnas.1016498108
发表时间:
2011-02-15
影响因子:
11.1
作者:
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通讯作者:
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DOI:
10.1083/jcb.139.5.1271
发表时间:
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期刊:
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影响因子:
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7.8
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通讯作者:
Hyman, Anthony
DOI:
10.1083/jcb.105.5.2203
发表时间:
1987-11
期刊:
The Journal of cell biology
影响因子:
--
作者:
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通讯作者:
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