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

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    Authors
    von Loeffelholz, O
    Venables, Neil A
    Drummond, D
    Katsuki, M
    Cross, R
    Moores, C
    Affiliation
    Institute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX,
    Issue Date
    2017-12-13
    
    Metadata
    Show full item record
    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.
    Citation
    Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics. 2017, 8(1): 2110 Nat Commun
    Journal
    Nature Communications
    URI
    http://hdl.handle.net/10541/620776
    DOI
    10.1038/s41467-017-02241-5
    PubMed ID
    29235477
    Type
    Article
    Language
    en
    ISSN
    2041-1723
    ae974a485f413a2113503eed53cd6c53
    10.1038/s41467-017-02241-5
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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