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dc.contributor.authorvon Loeffelholz, O
dc.contributor.authorVenables, Neil A
dc.contributor.authorDrummond, D
dc.contributor.authorKatsuki, M
dc.contributor.authorCross, R
dc.contributor.authorMoores, C
dc.date.accessioned2018-01-14T18:43:31Z
dc.date.available2018-01-14T18:43:31Z
dc.date.issued2017-12-13
dc.identifier.citationNucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics. 2017, 8(1): 2110 Nat Communen
dc.identifier.issn2041-1723
dc.identifier.pmid29235477
dc.identifier.doi10.1038/s41467-017-02241-5
dc.identifier.urihttp://hdl.handle.net/10541/620776
dc.description.abstractUsing 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.
dc.language.isoenen
dc.rightsArchived with thanks to Nature communicationsen
dc.titleNucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics.en
dc.typeArticleen
dc.contributor.departmentInstitute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX,en
dc.identifier.journalNature Communicationsen
refterms.dateFOA2018-12-17T15:11:39Z
html.description.abstractUsing 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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