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TitleMicrotubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry.
Journal, issue, pagesNature, Vol. 466, Issue 7308, Page 879-882, Year 2010
Publish dateAug 12, 2010
AuthorsJustin M Kollman / Jessica K Polka / Alex Zelter / Trisha N Davis / David A Agard /
PubMed AbstractMicrotubules are nucleated in vivo by gamma-tubulin complexes. The 300-kDa gamma-tubulin small complex (gamma-TuSC), consisting of two molecules of gamma-tubulin and one copy each of the accessory ...Microtubules are nucleated in vivo by gamma-tubulin complexes. The 300-kDa gamma-tubulin small complex (gamma-TuSC), consisting of two molecules of gamma-tubulin and one copy each of the accessory proteins Spc97 and Spc98, is the conserved, essential core of the microtubule nucleating machinery. In metazoa multiple gamma-TuSCs assemble with other proteins into gamma-tubulin ring complexes (gamma-TuRCs). The structure of gamma-TuRC indicated that it functions as a microtubule template. Because each gamma-TuSC contains two molecules of gamma-tubulin, it was assumed that the gamma-TuRC-specific proteins are required to organize gamma-TuSCs to match 13-fold microtubule symmetry. Here we show that Saccharomyces cerevisiae gamma-TuSC forms rings even in the absence of other gamma-TuRC components. The yeast adaptor protein Spc110 stabilizes the rings into extended filaments and is required for oligomer formation under physiological buffer conditions. The 8-A cryo-electron microscopic reconstruction of the filament reveals 13 gamma-tubulins per turn, matching microtubule symmetry, with plus ends exposed for interaction with microtubules, implying that one turn of the filament constitutes a microtubule template. The domain structures of Spc97 and Spc98 suggest functions for conserved sequence motifs, with implications for the gamma-TuRC-specific proteins. The gamma-TuSC filaments nucleate microtubules at a low level, and the structure provides a strong hypothesis for how nucleation is regulated, converting this less active form to a potent nucleator.
External linksNature / PubMed:20631709 / PubMed Central
MethodsEM (helical sym.)
Resolution8.0 Å
Structure data

EMDB-1731:
The microtubule nucleating gamma-tubulin small complex assembles into a structure with microtubule-like thirteen fold symmetry
Method: EM (helical sym.) / Resolution: 8.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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