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Architecture of the Mto1/2 microtubule nucleation complex

View ORCID ProfileHarish C. Thakur, View ORCID ProfileEric M. Lynch, View ORCID ProfileWeronika E. Borek, View ORCID ProfileXun X. Bao, View ORCID ProfileSanju Ashraf, View ORCID ProfileJuan Zou, View ORCID ProfileJuri Rappsilber, View ORCID ProfileAtlanta G. Cook, View ORCID ProfileKenneth E. Sawin
doi: https://doi.org/10.1101/754457
Harish C. Thakur
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Eric M. Lynch
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Weronika E. Borek
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Xun X. Bao
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Sanju Ashraf
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Juan Zou
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Juri Rappsilber
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UKChair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin 13355, Germany
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Atlanta G. Cook
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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Kenneth E. Sawin
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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  • For correspondence: ken.sawin@ed.ac.uk
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ABSTRACT

Proteins that contain a Centrosomin Motif 1 (CM1) domain are key regulators of γ-tubulin complex-dependent microtubule nucleation, but how they are organized in higher-order structures is largely unknown. Mto1[bonsai], a truncated functional version of the Schizosaccharomyces pombe CM1 protein Mto1, interacts with Mto2 to form an Mto1/2[bonsai] complex in vivo. Here we show that recombinant Mto1/2[bonsai] forms higher-order multimers in vitro and that Mto2 alone can also multimerize. We demonstrate that Mto2 multimerization involves two separate homodimerization domains, the near N-terminal domain (NND) and the twin-cysteine domain (TCD). The TCD crystal structure reveals a stable homodimer with a novel dimerization interface. While the NND homodimer is intrinsically less stable, using crosslinking mass spectrometry we show that within Mto1/2[bonsai] complexes, it can be reinforced by additional cooperative interactions involving both Mto2 and Mto1[bonsai]. We propose a model for Mto1/2[bonsai] complex architecture that is supported by functional analysis of mutants in vivo.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted August 31, 2019.
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Architecture of the Mto1/2 microtubule nucleation complex
Harish C. Thakur, Eric M. Lynch, Weronika E. Borek, Xun X. Bao, Sanju Ashraf, Juan Zou, Juri Rappsilber, Atlanta G. Cook, Kenneth E. Sawin
bioRxiv 754457; doi: https://doi.org/10.1101/754457
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Architecture of the Mto1/2 microtubule nucleation complex
Harish C. Thakur, Eric M. Lynch, Weronika E. Borek, Xun X. Bao, Sanju Ashraf, Juan Zou, Juri Rappsilber, Atlanta G. Cook, Kenneth E. Sawin
bioRxiv 754457; doi: https://doi.org/10.1101/754457

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