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-Structure paper
タイトル | Cryo-EM of α-tubulin isotype-containing microtubules revealed a contracted structure of α4A/β2A microtubules. |
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ジャーナル・号・ページ | Acta Biochim Biophys Sin (Shanghai), Vol. 55, Issue 10, Page 1551-1560, Year 2023 |
掲載日 | 2023年7月13日 |
著者 | Lei Diao / Wei Zheng / Qiaoyu Zhao / Mingyi Liu / Zhenglin Fu / Xu Zhang / Lan Bao / Yao Cong / |
PubMed 要旨 | Microtubules are hollow α/β-tubulin heterodimeric polymers that play critical roles in cells. In vertebrates, both α- and β-tubulins have multiple isotypes encoded by different genes, which are ...Microtubules are hollow α/β-tubulin heterodimeric polymers that play critical roles in cells. In vertebrates, both α- and β-tubulins have multiple isotypes encoded by different genes, which are intrinsic factors in regulating microtubule functions. However, the structures of microtubules composed of different tubulin isotypes, especially α-tubulin isotypes, remain largely unknown. Here, we purify recombinant tubulin heterodimers composed of different mouse α-tubulin isotypes, including α1A, α1C and α4A, with the β-tubulin isotype β2A. We further assemble and determine the cryo-electron microscopy (cryo-EM) structures of α1A/β2A, α1C/β2A, and α4A/β2A microtubules. Our structural analysis demonstrates that α4A/β2A microtubules exhibit longitudinal contraction between tubulin interdimers compared with α1A/β2A and α1C/β2A microtubules. Collectively, our findings reveal that α-tubulin isotype composition can tune microtubule structures, and also provide evidence for the "tubulin code" hypothesis. |
リンク | Acta Biochim Biophys Sin (Shanghai) / PubMed:37439022 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.2 - 4.4 Å |
構造データ | EMDB-35790: GMPCPP-Alpha1A/Beta2A-microtubule decorated with kinesin EMDB-35791: GMPCPP-Alpha1C/Beta2A-microtubule decorated with kinesin |
化合物 | ChemComp-GTP: ChemComp-G2P: ChemComp-ATP: |
由来 |
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キーワード | STRUCTURAL PROTEIN (タンパク質) / microtubule (微小管) / tubulin isotype / cryo-EM structure |