Nucleic Acids Research, Vol 24, Issue 12 2331-2337, Copyright © 1996 by Oxford University Press
A Rahner, A Scholer, E Martens, B Gollwitzer and HJ Schuller
The CSRE (carbon source-responsive element) is a sequence motif responsible
for the transcriptional activation of gluconeogenic structural genes in
Saccharomyces cerevisiae. We have isolated a regulatory gene, DIL1
(derepression of isocitrate lyase, = CAT8), which is specifically required
for derepression of CSRE-dependent genes. Expression of CAT8 is carbon
source regulated and requires a functional Cat1p (Snf1p) protein kinase.
The derepression defect of CAT8 in a cat1 mutant could be suppressed by a
mutant Mig1p repressor protein. Derepression of CAT8 also requires a
functional HAP2 gene, suggesting a regulatory connection between
respiratory and gluconeogenic genes. Carbon source-dependent protein-CSRE
complexes detected in a gel retardation analysis with wild-type extracts
were absent in cat8 mutant extracts. However, similar experiments with an
epitope-tagged CAT8 gene product in the presence of tag-specific antibodies
gave evidence against a direct binding of Cat8p to the CSRE. A
constitutively expressed GAL4-CAT8 fusion gene revealed a carbon
source-dependent transcriptional activation of a UAS(GAL)-containing
reporter gene. Activation mediated by Cat8p was no longer detectable in a
cat1 mutant. Thus, biosynthetic control of CAT8 as well as transcriptional
activation by Cat8p requires a functional Cat1p protein kinase. A model
proposing CAT8 as a specific activator of a transcription factor(s) binding
to the CSRE is discussed.
ARTICLES
Dual influence of the yeast Cat1p (Snf1p) protein kinase on carbon source-dependent transcriptional activation of gluconeogenic genes by the regulatory gene CAT8
Institut fur Mikrobiologie, Biochemie und Genetik, Lehrstuhl Biochemie, Universitat Erlangen/Nurnberg, Erlangen, Germany.
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