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-Structure paper
タイトル | Structural differences between yeast and mammalian microtubules revealed by cryo-EM. |
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ジャーナル・号・ページ | J Cell Biol, Vol. 216, Issue 9, Page 2669-2677, Year 2017 |
掲載日 | 2017年9月4日 |
著者 | Stuart C Howes / Elisabeth A Geyer / Benjamin LaFrance / Rui Zhang / Elizabeth H Kellogg / Stefan Westermann / Luke M Rice / Eva Nogales / |
PubMed 要旨 | Microtubules are polymers of αβ-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in ...Microtubules are polymers of αβ-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between αβ-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures. |
リンク | J Cell Biol / PubMed:28652389 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.7 - 6.0 Å |
構造データ | EMDB-8757, PDB-5w3j: EMDB-8758: EMDB-8759: |
化合物 | ChemComp-MG: ChemComp-GTP: ChemComp-GDP: ChemComp-EP: ChemComp-TA1: |
由来 |
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キーワード | HYDROLASE / Cytoskeleton / tubulin |