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Effects of α-tubulin acetylation on microtubule structure and stability

By Lisa Eshun-Wilson, Rui Zhang, Didier Portran, Maxence Nachury, Dan Toso, Thomas Lohr, Michele Vendruscolo, Massimiliano Bonomi, James S. Fraser, Eva Nogales

Posted 09 Jan 2019
bioRxiv DOI: 10.1101/516591 (published DOI: 10.1073/pnas.1900441116)

Acetylation of K40 in α-tubulin is the sole post-translational 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 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 the 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.

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