Journal
SCIENCE
Volume 319, Issue 5866, Pages 1090-1092Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1151903
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NCI NIH HHS [P30 CA045508] Funding Source: Medline
- NIGMS NIH HHS [GM074075, R01 GM074075, R01 GM074075-04, GM55641] Funding Source: Medline
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Transcriptional regulation of the galactose- metabolizing genes in Saccharomyces cerevisiae depends on three core proteins: Gal4p, the transcriptional activator that binds to upstream activating DNA sequences (UAS(GAL)); Gal80p, a repressor that binds to the carboxyl terminus of Gal4p and inhibits transcription; and Gal3p, a cytoplasmic transducer that, upon binding galactose and adenosine 5 '-triphosphate, relieves Gal80p repression. The current model of induction relies on Gal3p sequestering Gal80p in the cytoplasm. However, the rapid induction of this system implies that there is a missing factor. Our structure of Gal80p in complex with a peptide from the carboxyl- terminal activation domain of Gal4p reveals the existence of a dinucleotide that mediates the interaction between the two. Biochemical and in vivo experiments suggests that nicotinamide adenine dinucleotide phosphate ( NADP) plays a key role in the initial induction event.
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