Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3(Alp6).

Dhani, Deepsharan K, Goult, Benjamin T ORCID: 0000-0002-3438-2807, George, Gifty M, Rogerson, Daniel T, Bitton, Danny A, Miller, Crispin J ORCID: 0000-0003-4341-1283, Schwabe, John WR ORCID: 0000-0003-2865-4383 and Tanaka, Kayoko ORCID: 0000-0002-2905-3603 (2013) Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3(Alp6). Molecular biology of the cell, 24 (21). pp. 3337-3349.

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Official URL: http://dx.doi.org/10.1091/mbc.e13-05-0253

Abstract

In humans, MOZART1 plays an essential role in mitotic spindle formation as a component of the γ-tubulin ring complex. We report that the fission yeast homologue of MOZART1, Mzt1/Tam4, is located at microtubule-organizing centers (MTOCs) and coimmunoprecipitates with γ-tubulin Gtb1 from cell extracts. We show that mzt1/tam4 is an essential gene in fission yeast, encoding a 64-amino acid peptide, depletion of which leads to aberrant microtubule structure, including malformed mitotic spindles and impaired interphase microtubule array. Mzt1/Tam4 depletion also causes cytokinesis defects, suggesting a role of the γ-tubulin complex in the regulation of cytokinesis. Yeast two-hybrid analysis shows that Mzt1/Tam4 forms a complex with Alp6, a fission yeast homologue of γ-tubulin complex protein 3 (GCP3). Biophysical methods demonstrate that there is a direct interaction between recombinant Mzt1/Tam4 and the N-terminal region of GCP3(Alp6). Together our results suggest that Mzt1/Tam4 contributes to the MTOC function through regulation of GCP3(Alp6).

Item Type:	Article
Uncontrolled Keywords:	Microtubule-Organizing Center, Humans, Schizosaccharomyces, Tubulin, Microtubule-Associated Proteins, Schizosaccharomyces pombe Proteins, Green Fluorescent Proteins, Protein Subunits, Microscopy, Fluorescence, Blotting, Western, Two-Hybrid System Techniques, Binding Sites, Amino Acid Sequence, Protein Binding, Sequence Homology, Amino Acid, Molecular Sequence Data
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	13 Mar 2024 09:43
Last Modified:	13 Mar 2024 09:43
DOI:	10.1091/mbc.e13-05-0253
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3179340