ArticleProtein science : a publication of the Protein Society2017
NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.Science advances · 2026Article
- Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.Science advances · 2020Article
- The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.Nature communications · 2020Article
- Reconstitution of Microtubule Nucleation In Vitro Reveals Novel Roles for Mzt1.Current biology : CB · 2019Article
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
- Mitotic-Spindle Organizing Protein MztA Mediates Septation Signaling by Suppressing the Regulatory Subunit of Protein Phosphatase 2A-ParA inFrontiers in microbiology · 2018Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
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Abstract
Mitotic-spindle organizing protein associated with a ring of γ-tubulin 1 (MOZART1) is an 8.5 kDa protein linked to regulation of γ-tubulin ring complexes (γTuRCs), which are involved in nucleation of microtubules. Despite its small size, MOZART1 represents a challenging target for detailed characterization in vitro. We described herein a protocol for efficient production of recombinant human MOZART1 in Escherichia coli and assessed the properties of the purified protein using a combination of size exclusion chromatography coupled with multiangle light scattering (SEC-MALS), dynamic light scattering (DLS), and nuclear magnetic resonance (NMR) experiments. MOZART1 forms heterogeneous oligomers in solution. We identified optimal detergent and buffer conditions for recording well resolved NMR experiments allowing nearly full protein assignment and identification of three distinct alpha-helical structured regions. Finally, using NMR, we showed that MOZART1 interacts with the N-terminus (residues 1-250) of GCP3 (γ-tubulin complex protein 3). Our data illustrate the capacity of MOZART1 to form oligomers, promoting multiple contacts with a subset of protein partners in the context of microtubule nucleation.
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