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(Received for publication, July 10, 1995; and in revised form, August
11, 1995) A repeated element, the inositol-sensitive upstream activation
sequence (UAS In the present study, an extensive analysis
of UAS We also tested a subset of the altered elements for their ability to
serve as competitors in an assay of Ino2p
Volume 270,
Number 42,
Issue of October 20, 1995 pp. 25087-25095
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
A cis-REGULATORY ELEMENT RESPONSIBLE FOR INOSITOL-CHOLINE
MEDIATED REGULATION OF PHOSPHOLIPID BIOSYNTHESIS
), having the consensus sequence,
5`-CATGTGAAAT-3`, is present in the promoters of genes encoding enzymes
of phospholipid biosynthesis that are regulated in response to the
phospholipid precursors, inositol and choline. None of the naturally
occurring variants of the UAS
element exactly
recapitulates the consensus (for review, see Carman, G. M., and Henry,
S. A.(1989) Annu. Rev. Biochem. 58, 635-669 and Paltauf,
F., Kolwhein, S., and Henry, S. A.(1992) in Molecular Biology of
the Yeast Saccharomyces cerevisiae (Broach, J., Jones, E., and
Pringle, J., eds) Vol. 2, Cold Spring Harbor Laboratory, Cold Spring
Harbor, NY). The first six bases of the UAS
element are
homologous with canonical binding motif for proteins of the basic
helix-loop-helix (bHLH) family. Two bHLH regulatory proteins, Ino2p and
Ino4p from yeast, were previously shown to bind to promoter fragments
containing this element.
function has been conducted. We report that any
base substitution within the putative bHLH binding site resulted either
in a dramatic reduction or in a complete obliteration of UAS
function as tested in an expression assay in vivo. Base
substitutions in the 5` region that flanks the 10-base pair repeat, as
well as sequences within the repeat itself at its 3` end outside the
bHLH core, were also assessed. The two bases immediately flanking the
5` end of the element proved to be very important to its function as a
UAS element as did the two bases immediately 3` of the bHLH core motif.
Substitutions of the final two bases of the original ten base pair
consensus (i.e. 5`-CATGTGAAAT-3`) had less dramatic effects.
Ino4p binding. The
strength of any given sequence as a UAS element, as
assayed in vivo, was strongly correlated with its strength as
a competitor for Ino2p
Ino4p binding. We also tested a subset of
the modified UAS elements for their effects on expression in vivo in a strain carrying an opi1 mutation. The opi1 mutation renders the coregulated enzymes of phospholipid
synthesis constitutive in the presence of phospholipid precursors. All
elements that retained some residual UAS
activity when
tested in the wild-type strain were constitutively expressed at a level
comparable with the wild-type derepressed level when tested in the opi1 mutant. Thus, UAS
appears to be responsible
for OPI1 mediated repression, as well as Ino2p
Ino4p
binding. Furthermore, each of the identified functions of the
UAS element appears to have the same sequence
specificity, and all require the presence of the intact bHLH motif,
suggesting that transcriptional activation, repression, and
Ino2p
Ino4p binding are all components of a single regulatory
mechanism.
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