Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-02241-5
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Funding
- Biotechnology and Biological Sciences Research Council [BB/L00190X/1]
- Warwick Systems Biology DTC studentship [1090393]
- Wellcome Trust [103895/Z/14/Z]
- BBSRC [BB/L00190X/1, BB/L001993/1] Funding Source: UKRI
- MRC [G0200542] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L001993/1] Funding Source: researchfish
- Medical Research Council [G0200542] Funding Source: researchfish
- Wellcome Trust [103895/Z/14/Z] Funding Source: researchfish
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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-A 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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