Structural highlights
Publication Abstract from PubMed
A wealth of genetic information and some biochemical analysis have made the GAL regulon of the yeast Saccharomyces cerevisiae a classic model system for studying transcriptional activation in eukaryotes. Galactose induces this transcriptional switch, which is regulated by three proteins: the transcriptional activator Gal4p, bound to DNA; the repressor Gal80p; and the transducer Gal3p. We showed previously that NADP appears to act as a trigger to kick the repressor off the activator. Sustained activation involves a complex of the transducer Gal3p and Gal80p mediated by galactose and ATP. We solved the crystal structure of the complex of Gal3p-Gal80p with alpha-D-galactose and ATP to 2.1 A resolution. The interaction between the proteins occurs only when Gal3p is in a "closed" state induced by ligand binding. The structure of the complex provides a rationale for the phenotypes of several well-known Gal80p and Gal3p mutants as well as the lack of galactokinase activity of Gal3p.
The Gal3p transducer of the GAL regulon interacts with the Gal80p repressor in its ligand-induced closed conformation.,Lavy T, Kumar PR, He H, Joshua-Tor L Genes Dev. 2012 Feb 1;26(3):294-303. doi: 10.1101/gad.182691.111. PMID:22302941[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lavy T, Kumar PR, He H, Joshua-Tor L. The Gal3p transducer of the GAL regulon interacts with the Gal80p repressor in its ligand-induced closed conformation. Genes Dev. 2012 Feb 1;26(3):294-303. doi: 10.1101/gad.182691.111. PMID:22302941 doi:10.1101/gad.182691.111
