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-Structure paper
タイトル | Effects of α-tubulin acetylation on microtubule structure and stability. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 116, Issue 21, Page 10366-10371, Year 2019 |
掲載日 | 2019年5月21日 |
著者 | Lisa Eshun-Wilson / Rui Zhang / Didier Portran / Maxence V Nachury / Daniel B Toso / Thomas Löhr / Michele Vendruscolo / Massimiliano Bonomi / James S Fraser / Eva Nogales / |
PubMed 要旨 | Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule ...Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and acetylated states by using the experimental cryo-EM density as a structural restraint in molecular dynamics simulations. We found that acetylation alters the conformational landscape of the flexible loop that contains αK40. Modification of αK40 reduces the disorder of the loop and restricts the states that it samples. We propose that the change in conformational sampling that we describe, at a location very close to the lateral contacts site, is likely to affect microtubule stability and function. |
リンク | Proc Natl Acad Sci U S A / PubMed:31072936 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.3 - 4.1 Å |
構造データ | |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: |
由来 |
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キーワード | STRUCTURAL PROTEIN / microtubule / cytoskeleton / acetylation |