Previous Article | Next Article 
Mol Cell Biol. 1992 November; 12(11): 4981-4987
A transcriptionally active form of GAL4 is phosphorylated and associated with GAL80.
M R Parthun and
J A Jaehning
Department of Biology, Indiana University, Bloomington 47405.
ABSTRACT
The GAL4 activator and GAL80 repressor proteins regulate the expression of yeast genes in response to galactose. A complex of the two proteins isolated from glucose-grown cells is inactive in an in vitro transcription reaction but binds DNA and blocks activation by the GAL4-VP16 chimeric activator. The complex purified from galactose-grown cells contains a mixture of phosphorylated and unphosphorylated forms of GAL4. The galactose-induced form of GAL4 activates in vitro transcription to levels similar to those seen with GAL4-VP16. The induced GAL4 complex is indistinguishable in size and apparent shape from the uninduced complex, consistent with a continued association with GAL80. These results confirm in vivo analyses that correlate GAL4 phosphorylation with galactose induction and support a model of transcriptional activation that does not require GAL80 dissociation.
Mol Cell Biol. 1992 November; 12(11): 4981-4987
This article has been cited by other articles:
-
Wightman, R., Bell, R., Reece, R. J.
(2008). Localization and Interaction of the Proteins Constituting the GAL Genetic Switch in Saccharomyces cerevisiae. Eukaryot Cell
7: 2061-2068
[Abstract]
[Full Text]
-
Pilauri, V., Bewley, M., Diep, C., Hopper, J.
(2005). Gal80 Dimerization and the Yeast GAL Gene Switch. Genetics
169: 1903-1914
[Abstract]
[Full Text]
-
Larschan, E., Winston, F.
(2001). The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4. Genes Dev.
15: 1946-1956
[Abstract]
[Full Text]
-
Rohde, J. R., Trinh, J., Sadowski, I.
(2000). Multiple Signals Regulate GAL Transcription in Yeast. Mol. Cell. Biol.
20: 3880-3886
[Abstract]
[Full Text]
-
Huang, H. L., Brandriss, M. C.
(2000). The Regulator of the Yeast Proline Utilization Pathway Is Differentially Phosphorylated in Response to the Quality of the Nitrogen Source. Mol. Cell. Biol.
20: 892-899
[Abstract]
[Full Text]
-
Strouboulis, J., Damjanovski, S., Vermaak, D., Meric, F., Wolffe, A. P.
(1999). Transcriptional Repression by XPc1, a New Polycomb Homolog in Xenopus laevis Embryos, Is Independent of Histone Deacetylase. Mol. Cell. Biol.
19: 3958-3968
[Abstract]
[Full Text]
-
Hach, A., Hon, T., Zhang, L.
(1999). A New Class of Repression Modules Is Critical for Heme Regulation of the Yeast Transcriptional Activator Hap1. Mol. Cell. Biol.
19: 4324-4333
[Abstract]
[Full Text]
-
Su, K., Roos, M. D., Yang, X., Han, I., Paterson, A. J., Kudlow, J. E.
(1999). An N-terminal Region of Sp1 Targets Its Proteasome-dependent Degradation in Vitro. J. Biol. Chem.
274: 15194-15202
[Abstract]
[Full Text]
-
Yano, K.-i., Fukasawa, T.
(1997). Galactose-dependent reversible interaction of Gal3p with Gal80p in the induction pathway of Gal4p-activated genes of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA
94: 1721-1726
[Abstract]
[Full Text]
-
Habib, S., Hasnain, S. E.
(1996). A 38-kDa Host Factor Interacts with Functionally Important Motifs within the Autographa californica Multinucleocapsid Nuclear Polyhedrosis Virus Homologous Region (hr1) DNA Sequence. J. Biol. Chem.
271: 28250-28258
[Abstract]
[Full Text]
-
Chang, C., Gonzalez, F., Rothermel, B., Sun, L., Johnston, S. A., Kodadek, T.
(2001). The Gal4 Activation Domain Binds Sug2 Protein, a Proteasome Component, in Vivo and in Vitro. J. Biol. Chem.
276: 30956-30963
[Abstract]
[Full Text]