Academic literature on the topic 'Gal4/gal80'

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Journal articles on the topic "Gal4/gal80"

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Jiang, Fenglei, Benjamin R. Frey, Margery L. Evans, Jordan C. Friel, and James E. Hopper. "Gene Activation by Dissociation of an Inhibitor from a Transcriptional Activation Domain." Molecular and Cellular Biology 29, no. 20 (2009): 5604–10. http://dx.doi.org/10.1128/mcb.00632-09.

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ABSTRACT Gal4 is a prototypical eukaryotic transcriptional activator whose recruitment function is inhibited in the absence of galactose by the Gal80 protein through masking of its transcriptional activation domain (AD). A long-standing nondissociation model posits that galactose-activated Gal3 interacts with Gal4-bound Gal80 at the promoter, yielding a tripartite Gal3-Gal80-Gal4 complex with altered Gal80-Gal4 conformation to enable Gal4 AD activity. Some recent data challenge this model, whereas other recent data support the model. To address this controversy, we imaged fluorescent-protein-t
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Lue, N. F., D. I. Chasman, A. R. Buchman, and R. D. Kornberg. "Interaction of GAL4 and GAL80 gene regulatory proteins in vitro." Molecular and Cellular Biology 7, no. 10 (1987): 3446–51. http://dx.doi.org/10.1128/mcb.7.10.3446-3451.1987.

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The GAL80 protein of Saccharomyces cerevisiae, synthesized in vitro, bound tightly to GAL4 protein and to a GAL4 protein-upstream activation sequence DNA complex, as shown by (i) coimmunoprecipitation of GAL4 and GAL80 proteins with anti-GAL4 antiserum, (ii) an electrophoretic mobility shift of a GAL4 protein-upstream activation sequence DNA complex upon the addition of GAL80 protein, and (iii) GAL4-dependent binding of GAL80 protein to upstream activation sequence DNA immobilized on Sepharose beads. Anti-GAL4 antisera were raised against a GAL4-URA3 fusion protein, which could be purified to
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Lue, N. F., D. I. Chasman, A. R. Buchman, and R. D. Kornberg. "Interaction of GAL4 and GAL80 gene regulatory proteins in vitro." Molecular and Cellular Biology 7, no. 10 (1987): 3446–51. http://dx.doi.org/10.1128/mcb.7.10.3446.

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The GAL80 protein of Saccharomyces cerevisiae, synthesized in vitro, bound tightly to GAL4 protein and to a GAL4 protein-upstream activation sequence DNA complex, as shown by (i) coimmunoprecipitation of GAL4 and GAL80 proteins with anti-GAL4 antiserum, (ii) an electrophoretic mobility shift of a GAL4 protein-upstream activation sequence DNA complex upon the addition of GAL80 protein, and (iii) GAL4-dependent binding of GAL80 protein to upstream activation sequence DNA immobilized on Sepharose beads. Anti-GAL4 antisera were raised against a GAL4-URA3 fusion protein, which could be purified to
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Salmeron, J. M., S. D. Langdon, and S. A. Johnston. "Interaction between transcriptional activator protein LAC9 and negative regulatory protein GAL80." Molecular and Cellular Biology 9, no. 7 (1989): 2950–56. http://dx.doi.org/10.1128/mcb.9.7.2950-2956.1989.

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In Saccharomyces cerevisiae, transcriptional activation mediated by the GAL4 regulatory protein is repressed in the absence of galactose by the binding of the GAL80 protein, an interaction that requires the carboxy-terminal 28 amino acids of GAL4. The homolog of GAL4 from Kluyveromyces lactis, LAC9, activates transcription in S. cerevisiae and is highly similar to GAL4 in its carboxyl terminus but is not repressed by wild-type levels of GAL80 protein. Here we show that GAL80 does repress LAC9-activated transcription in S. cerevisiae if overproduced. We sought to determine the molecular basis f
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Salmeron, J. M., S. D. Langdon, and S. A. Johnston. "Interaction between transcriptional activator protein LAC9 and negative regulatory protein GAL80." Molecular and Cellular Biology 9, no. 7 (1989): 2950–56. http://dx.doi.org/10.1128/mcb.9.7.2950.

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In Saccharomyces cerevisiae, transcriptional activation mediated by the GAL4 regulatory protein is repressed in the absence of galactose by the binding of the GAL80 protein, an interaction that requires the carboxy-terminal 28 amino acids of GAL4. The homolog of GAL4 from Kluyveromyces lactis, LAC9, activates transcription in S. cerevisiae and is highly similar to GAL4 in its carboxyl terminus but is not repressed by wild-type levels of GAL80 protein. Here we show that GAL80 does repress LAC9-activated transcription in S. cerevisiae if overproduced. We sought to determine the molecular basis f
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Bhat, P. J., and J. E. Hopper. "Overproduction of the GAL1 or GAL3 protein causes galactose-independent activation of the GAL4 protein: evidence for a new model of induction for the yeast GAL/MEL regulon." Molecular and Cellular Biology 12, no. 6 (1992): 2701–7. http://dx.doi.org/10.1128/mcb.12.6.2701-2707.1992.

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The transcriptional activation function of the Saccharomyces cerevisiae GAL4 protein is modulated by the GAL80 and GAL3 proteins. In the absence of galactose, GAL80 inhibits the function of GAL4, presumably by direct binding to the GAL4 protein. The presence of galactose triggers the relief of the GAL80 block. The key to this relief is the GAL3 protein. How GAL3 and galactose activate GAL4 is not understood, but the long-standing notion has been that a galactose derivative formed by catalytic activity of GAL3 is the inducer that interacts with GAL80 or the GAL80-GAL4 complex. Here we report th
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Bhat, P. J., and J. E. Hopper. "Overproduction of the GAL1 or GAL3 protein causes galactose-independent activation of the GAL4 protein: evidence for a new model of induction for the yeast GAL/MEL regulon." Molecular and Cellular Biology 12, no. 6 (1992): 2701–7. http://dx.doi.org/10.1128/mcb.12.6.2701.

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The transcriptional activation function of the Saccharomyces cerevisiae GAL4 protein is modulated by the GAL80 and GAL3 proteins. In the absence of galactose, GAL80 inhibits the function of GAL4, presumably by direct binding to the GAL4 protein. The presence of galactose triggers the relief of the GAL80 block. The key to this relief is the GAL3 protein. How GAL3 and galactose activate GAL4 is not understood, but the long-standing notion has been that a galactose derivative formed by catalytic activity of GAL3 is the inducer that interacts with GAL80 or the GAL80-GAL4 complex. Here we report th
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Parthun, M. R., and J. A. Jaehning. "A transcriptionally active form of GAL4 is phosphorylated and associated with GAL80." Molecular and Cellular Biology 12, no. 11 (1992): 4981–87. http://dx.doi.org/10.1128/mcb.12.11.4981-4987.1992.

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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 appar
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Parthun, M. R., and J. A. Jaehning. "A transcriptionally active form of GAL4 is phosphorylated and associated with GAL80." Molecular and Cellular Biology 12, no. 11 (1992): 4981–87. http://dx.doi.org/10.1128/mcb.12.11.4981.

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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 appar
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Salmeron, J. M., K. K. Leuther, and S. A. Johnston. "GAL4 mutations that separate the transcriptional activation and GAL80-interactive functions of the yeast GAL4 protein." Genetics 125, no. 1 (1990): 21–27. http://dx.doi.org/10.1093/genetics/125.1.21.

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Abstract The carboxy-terminal 28 amino acids of the Saccharomyces cerevisiae transcriptional activator protein GAL4 execute two functions--transcriptional activation and interaction with the negative regulatory protein, GAL80. Here we demonstrate that these two functions are separable by single amino acid changes within this region. We determined the sequences of four GAL4C-mutations, and characterized the abilities of the encoded GAL4C proteins to activate transcription of the galactose/melibiose regulon in the presence of GAL80 and superrepressible GAL80S alleles. One of the GAL4C mutations
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Dissertations / Theses on the topic "Gal4/gal80"

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Goupil, Alix. "Genome instability : from genome content variations to gene expression plasticity." Electronic Thesis or Diss., Université Paris sciences et lettres, 2021. http://www.theses.fr/2021UPSLS053.

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La plupart de nos cellules sont diploïdes possédant deux copies de chaque chromosome. Lors de la mitose, la formation d’un fuseau bipolaire avec un centrosome à chaque pôle permet la ségrégation correcte des chromosomes, essentiel au maintien de la stabilité génétique. Il existe néanmoins des variations du contenu chromosomique comme la polyploïdie, définit comme le doublement de l’ensemble des chromosomes et l’aneuploïdie, définie comme la perte ou le gain de chromosome entier. Bien qu’observées, la fréquence des cellules aneuploïdies dans les tissus d’un organisme sain reste controversée.De
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Egriboz, Onur. "THE MOLECULAR MECHANISMS GOVERNING THE GAL GENE SWITCH OF SACCHAROMYCES CEREVISIAE." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1338319985.

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Goswami, Sudip. "Investigation Of The Behavior Of The Gal4 Inhibitor Gal80 Of The GAL Genetic Switch In The Yeast Saccharomyces Cerevisiae." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1408542557.

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Zugowski, Constance [Verfasser], K. [Akademischer Betreuer] Breunig, H. [Akademischer Betreuer] Lilie, and K. [Akademischer Betreuer] Melcher. "Molecular genetic and biochemical interaction studies of the transcriptional activator Gal4 and its repressor Gal80 in Saccharomyces cerevisiae and Kluyveromyces lactis / Constance Zugowski. Betreuer: K. Breunig ; H. Lilie ; K. Melcher." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2013. http://d-nb.info/1033306649/34.

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Anders, Alexander [Verfasser]. "Molekularer Mechanismus eines Transkriptionsschalters : experimentelle Analyse und mathematische Modellierung des Gal4-Gal80-Gal1-Regulationsmoduls aus Kluyveromyces lactis / von Alexander Anders." 2006. http://d-nb.info/985265698/34.

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