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Regulation of the yeast SPS19 gene encoding peroxisomal 2,4‐dienoyl‐CoA reductase by the transcription factors Pip2p and Oaf1p: β‐oxidation is dispensable for Saccharomyces cerevisiae sporulation in acetate medium
Author(s) -
Gurvitz Aner,
Rottensteiner Hanspeter,
Hiltunen J. Kalervo,
Binder Maximilian,
Dawes Ian W.,
Ruis Helmut,
Hamilton Barbara
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.5931969.x
Subject(s) - biology , peroxisome , saccharomyces cerevisiae , gene , transcription (linguistics) , reductase , yeast , reporter gene , transcription factor , biochemistry , microbiology and biotechnology , gene expression , enzyme , philosophy , linguistics
The yeast SPS19 gene encoding the peroxisomally targeted 2,4‐dienoyl‐CoA reductase shares its promoter region (291 bp) with the sporulation‐specific gene SPS18. SPS19 is induced during sporulation in diploids but to a lesser extent than SPS18 ; under oleate induction conditions, SPS19 , but not SPS18 , is transcribed via an oleate response element (ORE) independently of ploidy or sporulation. The SPS19 ORE is the binding target of the Pip2p and Oaf1p transcription factors, and an SPS19–lacZ reporter gene, which is highly expressed in oleate‐induced cells, is not activated in haploids devoid of either protein. We examined the expression of CYC1–lacZ reporter constructs carrying the SPS19 and CTA1 OREs in diploids propagated under sporulation conditions and have shown that OREs are not sufficient for heterologous expression during yeast development. In addition, diploids deleted at either PIP2 or OAF1 demonstrated abundant ascosporogenesis, indicating that these genes are not essential for sporulation. A Δ pex6 strain lacking peroxisomal structures and one devoid of fatty acyl‐CoA oxidase (Δ pox1 ), the first step in fungal β‐oxidation, were both proficient for sporulation and, hence, β‐oxidation and the peroxisomal compartment containing it are dispensable for meiotic development.