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Nat Commun. 2017 Dec 13;8(1):2110. doi: 10.1038/s41467-017-02241-5.

Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics.

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Institute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, UK.
Centre for Integrative Biology, Department of Integrated Structural Biology, Institute of Genetics and of Molecular and Cellular Biology, 1 rue Laurent Fries, Illkirch, France.
Division of Biomedical Cell Biology, Warwick Medical School, CV4 7AL, Coventry, UK.
CRUK Manchester Institute, The University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Centre for Promotion of International Education and Research, Faculty of Agriculture, Kyushu University, Fukuoka, 812-8581, Japan.
Department of Earth System Science, Faculty of Science, Fukuoka University, Fukuoka, 814-0180, Japan.
Institute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, UK.


Using cryo-electron microscopy, we characterize the architecture of microtubules assembled from Schizosaccharomyces pombe tubulin, in the presence and absence of their regulatory partner Mal3. Cryo-electron tomography reveals that microtubules assembled from S. pombe tubulin have predominantly B-lattice interprotofilament contacts, with protofilaments skewed around the microtubule axis. Copolymerization with Mal3 favors 13 protofilament microtubules with reduced protofilament skew, indicating that Mal3 adjusts interprotofilament interfaces. A 4.6-Å resolution structure of microtubule-bound Mal3 shows that Mal3 makes a distinctive footprint on the S. pombe microtubule lattice and that unlike mammalian microtubules, S. pombe microtubules do not show the longitudinal lattice compaction associated with EB protein binding and GTP hydrolysis. Our results firmly support a structural plasticity view of microtubule dynamics in which microtubule lattice conformation is sensitive to a variety of effectors and differently so for different tubulins.

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