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

Ottilie Von Loeffelholz, Neil A. Venables, Douglas Robert Drummond, Miho Katsuki, Robert Cross, Carolyn A. Moores

    Research output: Contribution to journalArticlepeer-review

    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.

    Original languageEnglish
    Article number2241
    JournalNature Communications
    Volume8
    Issue number1
    Early online date13 Dec 2017
    DOIs
    Publication statusPublished - Dec 2017

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