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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2002-05, Vol.293 (2), p.733-740
Main Authors: Park, Young-Un, Hwang, Oksun, Kim, Jinmi
Format: Article
Language:English
Subjects:
Carrier Proteins - genetics
Carrier Proteins - physiology
Cell Nucleus - metabolism
Cloning, Molecular
DEAD-box RNA Helicases
Filamentation
KEM1
Mating Factor
Membrane Fusion
Mutation
Nuclear fusion
OSH3
Oxysterol-binding protein
Peptides - pharmacology
RNA Helicases - metabolism
RNA, Fungal - biosynthesis
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - growth & development
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - physiology
Two-Hybrid System Techniques
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Summary: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 α-mating pheromone. We also found that OSH3 overexpression promoted filamentation growth of the Σ1278b 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(02)00288-7