Novel WD-repeat protein Mip1p facilitates function of the meiotic regulator Mei2p in fission yeast.

In fission yeast, the onset of meiosis is triggered by activation of the RNA-binding protein Mei2p. We screened for a high-copy-number suppressor of the ectopic meiosis induced by expression of an active form of Mei2p. Consequently we isolated a truncated form of a novel gene, named mip1, from a fission yeast genomic library. The mip1 gene encoded a protein of 1,313 amino acids which carried a WD-repeat motif in the C-terminal region and was apparently conserved among eukaryotes. Mip1p was cytoplasmic, and two-hybrid and immunoprecipitation analyses demonstrated that Mip1p was bound to Mei2p in vivo. Genetic evidence indicated that wild-type Mip1p was required for the function of Mei2p to induce meiosis and that the truncated form of it (Mip1-15p) dominantly interfered with Mei2p. Mip1p appeared to be involved also in conjugation, associating with Ste11p, which is a key transcription factor for sexual development. Furthermore, Mip1p was essential for cell growth, to which neither Mei2p nor Ste11p is relevant. These results suggest that Mip1p assists functional expression of a number of proteins required for proliferation and sexual development in fission yeast.