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

• Published in: Molecular biology of the cell 2013-11, Vol.24 (21), p.3337-3349
• Main Authors: Dhani, Deepsharan K., Goult, Benjamin T., George, Gifty M., Rogerson, Daniel T., Bitton, Danny A., Miller, Crispin J., Schwabe, John W. R., Tanaka, Kayoko
• Format: Article
• Language: English
• ISSN: 1059-1524; 1939-4586
• DOI: 10.1091/mbc.e13-05-0253

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 .