Now read this abstract from a 2013 journal article What is the authors' explanation of how Gal80p works? Note UASG from the question above is the same as UASGAL The DNA-binding transcriptional activator Gal4 and its regulators Gal80 and Gal3 constitute a galactose-responsive switch for the GAL genes of Saccharomyces cerevisiae. Gal4 binds to GAL gene UASLAL (upstream activation sequence in GAL gene pro- moter) sites as a dimer via its N-terminal domain and activates transcription via a C-terminal transcription activation domain (AD). In the absence of galactose, a Gal80 dimer binds to a dimer of Gal4, masking the Gal4AD. Galactose triggers Gal3-Gal80 interaction to rapidly initiate Gal4-mediated transcription activation. Just how Gal3 alters Gal80 to relieve Gal80 inhibition of Gald has been unknown, but previous analyses of Gal80 mutants suggested a possible competition between Gal3-Gal80 and Gals0 self-association interactions. Here we assayed Galso-Gal80 interactions and tested for effects of Gal3. Immunoprecipita- tion, cross-linking, and denaturing and native PAGE analyses of Gal80 in vitro and fluorescence imaging of Gal80 in live cells show that Gal3-Gal80 interaction occurs concomitantly with a decrease in Gal80 multimers. Consistent with this, we find that newly discovered nuclear clusters of Gal80 dissipate in response to galactose-triggered Gal3-Gal80 interaction. We discuss the effect of Gal3 on the quaternary structure of Galso in light of the evidence pointing to multimeric Gal80 as the form required to inhibit Gal4. O Gal80p dimers block the Gal4p transcription activation domain (AD). When galactose is added, Gal3 protein binds Gal80p and prevents its dimerization. When galactose is added the Gal80p prevents Gal4p from binding at the UAS. Gal4p cycles between dimers with an available transcription activation domain (AD) and monomers without an AD.
Now read this abstract from a 2013 journal article What is the authors' explanation of how Gal80p works? Note UASG from the question above is the same as UASGAL The DNA-binding transcriptional activator Gal4 and its regulators Gal80 and Gal3 constitute a galactose-responsive switch for the GAL genes of Saccharomyces cerevisiae. Gal4 binds to GAL gene UASLAL (upstream activation sequence in GAL gene pro- moter) sites as a dimer via its N-terminal domain and activates transcription via a C-terminal transcription activation domain (AD). In the absence of galactose, a Gal80 dimer binds to a dimer of Gal4, masking the Gal4AD. Galactose triggers Gal3-Gal80 interaction to rapidly initiate Gal4-mediated transcription activation. Just how Gal3 alters Gal80 to relieve Gal80 inhibition of Gald has been unknown, but previous analyses of Gal80 mutants suggested a possible competition between Gal3-Gal80 and Gals0 self-association interactions. Here we assayed Galso-Gal80 interactions and tested for effects of Gal3. Immunoprecipita- tion, cross-linking, and denaturing and native PAGE analyses of Gal80 in vitro and fluorescence imaging of Gal80 in live cells show that Gal3-Gal80 interaction occurs concomitantly with a decrease in Gal80 multimers. Consistent with this, we find that newly discovered nuclear clusters of Gal80 dissipate in response to galactose-triggered Gal3-Gal80 interaction. We discuss the effect of Gal3 on the quaternary structure of Galso in light of the evidence pointing to multimeric Gal80 as the form required to inhibit Gal4. O Gal80p dimers block the Gal4p transcription activation domain (AD). When galactose is added, Gal3 protein binds Gal80p and prevents its dimerization. When galactose is added the Gal80p prevents Gal4p from binding at the UAS. Gal4p cycles between dimers with an available transcription activation domain (AD) and monomers without an AD.
Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Gene Interactions
When the expression of a single trait is influenced by two or more different non-allelic genes, it is termed as genetic interaction. According to Mendel's law of inheritance, each gene functions in its own way and does not depend on the function of another gene, i.e., a single gene controls each of seven characteristics considered, but the complex contribution of many different genes determine many traits of an organism.
Gene Expression
Gene expression is a process by which the instructions present in deoxyribonucleic acid (DNA) are converted into useful molecules such as proteins, and functional messenger ribonucleic (mRNA) molecules in the case of non-protein-coding genes.
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Transcribed Image Text:Now read this abstract from a 2013 journal article What is the authors' explanation of how Gal80p works?
Note UASG from the question above is the same as UASGAL
The DNA-binding transcriptional activator Gal4 and its regulators Gal80 and Gal3 constitute a galactose-responsive switch for
the GAL genes of Saccharomyces cerevisiae. Gal4 binds to GAL gene UASGAL. (upstream activation sequence in GAL gene pro-
moter) sites as a dimer via its N-terminal domain and activates transcription via a C-terminal transcription activation domain
(AD). In the absence of galactose, a Gal80 dimer binds to a dimer of Gal4, masking the Gal4AD. Galactose triggers Gal3-Gal80
interaction to rapidly initiate Gal4-mediated transcription activation. Just how Gal3 alters Gal80 to relieve Gals0 inhibition of
Gal4 has been unknown, but previous analyses of Gal80 mutants suggested a possible competition between Gal3-Gal80 and
Gal80 self-association interactions. Here we assayed Gal80-Gal80 interactions and tested for effects of Gal3. Immunoprecipita-
tion, cross-linking, and denaturing and native PAGE analyses of Gal80 in vitro and fluorescence imaging of Gal80 in live cells
show that Gal3-Gal80 interaction occurs concomitantly witha decrease in Gals0 multimers. Consistent with this, we find that
newly discovered nuclear clusters of Gal80 dissipate in response to galactose-triggered Gal3-Gal80 interaction. We discuss the
effect of Gal3 on the quaternary structure of Gal80 in light of the evidence pointing to multimeric Gal80 as the form required to
inhibit Gal4.
Gal80p dimers block the Gal4p transcription activation domain (AD). When galactose is added, Gal3
protein binds Gal80p and prevents its dimerization.
When galactose is added the Gal80p prevents Gal4p from binding at the UAS.
O Gal4p cycles between dimers with an available transcription activation domain (AD) and monomers
without an AD.
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