1. Spo5/Mug12, a Putative Meiosis-Specific RNA-Binding Protein, Is Essential for Meiotic Progression and Forms Mei2 Dot-Like Nuclear Foci†
- Author
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Akira Shigehisa, Takamune T. Saito, Aiko Hirata, Takahiro Tougan, Takashi Kasama, Daisuke Okuzaki, and Hiroshi Nojima
- Subjects
Cyclin-dependent kinase 1 ,Molecular Sequence Data ,RNA-Binding Proteins ,RNA-binding protein ,General Medicine ,Articles ,Biology ,Spores, Fungal ,biology.organism_classification ,Microbiology ,Molecular biology ,Green fluorescent protein ,Meiosis ,Cytoplasm ,Schizosaccharomyces pombe ,Mutation ,Schizosaccharomyces ,Amino Acid Sequence ,Schizosaccharomyces pombe Proteins ,Molecular Biology ,Sequence Alignment ,Immunostaining ,Anaphase - Abstract
We report here a functional analysis of spo5 + ( mug12 + ) of Schizosaccharomyces pombe , which encodes a putative RNA-binding protein. The disruption of spo5 + caused abnormal sporulation, generating inviable spores due to failed forespore membrane formation and the absence of a spore wall, as determined by electron microscopy. Spo5 regulates the progression of meiosis I because spo5 mutant cells display normal premeiotic DNA synthesis and the timely initiation of meiosis I but they show a delay in the peaking of cells with two nuclei, abnormal tyrosine 15 dephosphorylation of Cdc2, incomplete degradation of Cdc13, retarded formation and repair of double strand breaks, and a reduced frequency of intragenic recombination. Immunostaining showed that Spo5-green fluorescent protein (GFP) appeared in the cytoplasm at the horsetail phase, peaked around the metaphase I to anaphase I transition, and suddenly disappeared after anaphase II. Images of Spo5-GFP in living cells revealed that Spo5 forms a dot in the nucleus at prophase I that colocalized with the Mei2 dot. Unlike the Mei2 dot, however, the Spo5 dot was observed even in sme2Δ cells. Taken together, we conclude that Spo5 is a novel regulator of meiosis I and that it may function in the vicinity of the Mei2 dot.
- Published
- 2006