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J. Biol. Chem., Vol. 266, Issue 2, 863-872, 01, 1991
MJ White, JP Hirsch and SA Henry
In Saccharomyces cerevisiae, recessive mutations at the OPI1 locus result
in constitutively derepressed expression of inositol 1-phosphate synthase,
the product of the INO1 gene. Many of the other enzymes involved in
phospholipid biosynthesis are also expressed at high derepressed levels in
opi1 mutants. Thus, the OPI1 gene is believed to encode a negative
regulator that is required to repress a whole subset of structural genes
encoding for phospholipid biosynthetic enzymes. In this study, the OPI1
gene was mapped to chromosome VIII and cloned. When transformed into an
opi1 mutant, the cloned DNA was capable of complementing the mutant
phenotype and restoring correct regulation to the INO1 structural gene.
Construction of two opi1 disruption alleles and subsequent genetic analysis
of strains bearing these alleles confirmed that the cloned DNA was
homologous to the genomic OPI1 locus. Furthermore, the OPI1 gene was found
to be nonessential to the organism since mutants bearing the null allele
were viable and exhibited a phenotype similar to that of previously
isolated opi1 mutants. Similar to other opi1 mutants, the opi1 disruption
mutants accumulated INO1 mRNA constitutively to a level 2-3-fold higher
than that observed in wild-type cells. The cloned OPI1 gene was sequenced,
and translation of the open reading frame predicted a protein composed of
404 amino acid residues with a molecular weight of 40,036. The predicted
Opi1 protein contained a well defined heptad repeat of leucine residues
that has been observed in other regulatory proteins. In addition, the
predicted protein contained polyglutamine residue stretches which have also
been reported in yeast genes having regulatory functions. Sequencing of
opi1 mutant alleles, isolated after chemical mutagenesis, revealed that
several were the result of a chain termination mutation located within the
largest polyglutamine residue stretch.
The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of phospholipid biosynthesis, encodes a protein containing polyglutamine tracts and a leucine zipper
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
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