Two-hybrid cloning and characterization of OSH3, a yeast oxysterol-binding protein homolog.

Biochem Biophys Res Commun

Department of Microbiology, College of Natural Sciences, Chungnam National University, Taejeon 305-764, Republic of Korea.

Published: May 2002

AI Article Synopsis

  • Osh3p, a yeast oxysterol-binding protein homolog, interacts with the DEAD-box RNA helicase Rok1p, suggesting a role in RNA processing or regulation.
  • The ROK1 gene can suppress nuclear fusion defects caused by a kem1 mutation, indicating a connection between these proteins and cellular fusion processes.
  • High levels of Osh3p expression, triggered by alpha-mating pheromone, influence yeast growth and development, particularly in filamentation and nuclear fusion.

Article Abstract

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.

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Source
http://dx.doi.org/10.1016/S0006-291X(02)00288-7DOI Listing

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