Proteomics

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Reconstitution of microtubule nucleation in vitro reveals novel roles for Mzt1

ABSTRACT: Protein-protein interaction within the MGM holocomplex has been investigated by chemical cross-linking mass spectrometry using EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) cross-linker. Although this analysis was not exhaustive, we observed crosslinks between Alp4 and Alp6 along the length of these two proteins, consistent with their general parallel lateral alignment in current models for gamma-TuC organization. In addition, we observed specific cross-links from both Alp4 and Alp6 to the Mto1 [bonsai] CM1 domain and/or its immediate flanking regions. Interestingly, crosslinks from Alp4 and Alp6 N-terminal regions tended to be to the C-terminal portion of the CM1 domain, while crosslinks from Alp4 and Alp6 C-terminal regions tended to be to the N-terminal portion of the CM1 domain. This raises the possibility that the CM1 domain, which is adjacent to coiled-coil regions, may be oriented antiparallel to Alp4 and Alp6.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Schizosaccharomyces Pombe

SUBMITTER: Juan Zou  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD012624 | Pride | 2019-05-27

REPOSITORIES: Pride

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Reconstitution of Microtubule Nucleation In Vitro Reveals Novel Roles for Mzt1.

Leong Su Ling SL   Lynch Eric M EM   Zou Juan J   Tay Ye Dee YD   Borek Weronika E WE   Tuijtel Maarten W MW   Rappsilber Juri J   Sawin Kenneth E KE  

Current biology : CB 20190701 13

Microtubule (MT) nucleation depends on the γ-tubulin complex (γ-TuC), in which multiple copies of the heterotetrameric γ-tubulin small complex (γ-TuSC) associate to form a ring-like structure (in metazoans, γ-tubulin ring complex; γ-TuRC) [1-7]. Additional conserved regulators of the γ-TuC include the small protein Mzt1 (MOZART1 in human; GIP1/1B and GIP2/1A in plants) [8-13] and proteins containing a Centrosomin Motif 1 (CM1) domain [10, 14-19]. Many insights into γ-TuC regulators have come fro  ...[more]

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