Two-hybrid cloning and characterization of OSH3, a yeast oxysterol-binding protein homolog.
We identify Osh3p, one of seven yeast oxysterol-binding protein (OSBP) homologs, by its protein-protein interactions with a DEAD-box RNA helicase, Rok1p. The ROK1 gene was initially identified by its ability on a high-copy number plasmid to suppress the nuclear fusion defect caused by the kem1 null mutation. Our results show that OSH3 also affects nuclear fusion in a kem1-specific manner; the nuclear fusion defect of kem1 was intensified by the multicopy expression of OSH3. The Osh3p synthesis was highly induced by alpha-mating pheromone. We also found that OSH3 overexpression promoted filamentation growth of the Sigma1278b wild-type strain and suppressed the filamentation growth defect of the ste12 mutation. These results lead us to a new understanding of cellular functions of the yeast OSBPs.[1]References
- Two-hybrid cloning and characterization of OSH3, a yeast oxysterol-binding protein homolog. Park, Y.U., Hwang, O., Kim, J. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
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