A TOG

αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase

Pelin Ayaz, Xuecheng Ye, Patrick Huddleston, Chad A Brautigam, Luke M Rice

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)857-860
Number of pages4
JournalScience
Volume337
Issue number6096
DOIs
StatePublished - Aug 17 2012

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Tubulin
Microtubules
Genes
Neoplasms
Catalysis
Yeasts
Growth

ASJC Scopus subject areas

  • General

Cite this

A TOG : αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. / Ayaz, Pelin; Ye, Xuecheng; Huddleston, Patrick; Brautigam, Chad A; Rice, Luke M.

In: Science, Vol. 337, No. 6096, 17.08.2012, p. 857-860.

Research output: Contribution to journalArticle

Ayaz, Pelin ; Ye, Xuecheng ; Huddleston, Patrick ; Brautigam, Chad A ; Rice, Luke M. / A TOG : αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. In: Science. 2012 ; Vol. 337, No. 6096. pp. 857-860.
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