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

    von Loeffelholz, Ottie and Venables, N.A. and Drummond, D.R. and Katsuki, M. and Cross, R. and Moores, Carolyn A. (2017) Nucleotide– and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics. Nature Communications 8 (1), ISSN 2041-1723.

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    Abstract

    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 13 Dec 2017 14:03
    Last Modified: 30 Jul 2019 12:27
    URI: http://eprints.bbk.ac.uk/id/eprint/20623

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