TY - JOUR
T1 - Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics
AU - Von Loeffelholz, Ottilie
AU - Venables, Neil A.
AU - Drummond, Douglas Robert
AU - Katsuki, Miho
AU - Cross, Robert
AU - Moores, Carolyn A.
N1 - Funding Information:
O.v.L. and C.A.M. were supported by Biotechnology and Biological Sciences Research Council (BB/L00190X/1), and thank Dr Dan Clare for technical help with cryo-EM, Dr Claire Naylor for help with model building, and the wider Birkbeck EM community at Birkbeck for helpful discussions. R.C. thanks Dr Anne Straube for the gift of EB1-GFP. N.A.V. was supported by a Warwick Systems Biology DTC studentship, grant number 1090393. R.C. is supported by a Wellcome Trust Senior Investigator Award (grant number 103895/Z/14/Z).
Publisher Copyright:
© 2017 The Author(s).
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
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U2 - 10.1038/s41467-017-02241-5
DO - 10.1038/s41467-017-02241-5
M3 - Article
C2 - 29235477
AN - SCOPUS:85038437373
VL - 8
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 2110
ER -