Analysis of Aspergillus nidulans homolog of Mozart1, a newly identified spindle pole protein.

Tetsuya Horio1, Takashi Toda2 and Berl R. Oakley1

Author address: 

1Department of Molecular Biosciences, University of Kansas, Lawrence, KS. 2Cancer Research UK, London Research Institute, London, UK.


Mozart1 is a small centrosomal protein (82 aa) which was newly identified by high-throughput genome-wide screening of animal cells. It plays an important role in mitosis (Hutchins et al., Science 2010, 328, 593-). A homolog of Mozart1 (mztA) that exhibits about 50% amino acid identity is encoded by a single gene in A. nidulans. Tagging MZTA with fluorescent proteins revealed that MZTA localizes to spindle pole bodies indicating that this polypeptide is likely to be an functional homolog of Mozart1. Strains carrying a deletion of mztA were viable but exhibited a weak temperature sensitivity. In mztA deletants, fewer cytoplasmic microtubules were observed suggesting that nucleation of the microtubules is suppressed in the absence of the MZTA. We investigated the functional relationship between MZTA and the (-tubulin complex proteins (GCPs). Double deletion of mztA and nonessential GCP genes (gcpD-F) exhibited a variety of synthetically sick phenotypes. While the absence of these nonessential GCPs does not affect growth significantly, depleting both MZTA and one of these GCPs at the same time caused a significant growth reduction. Our data indicates that the MZTA plays an important role in organizing the microtubules in A. nidulans by interacting with (-tubulin and/or (-tubulin complex proteins.

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Full conference title: 

26th Fungal Genetics Conference
    • Fungal Genetics Conference 26th (2005)