Promoter Binding by the Adr1 Transcriptional Activator May Be Regulated by Phosphorylation in the DNA-Binding Region
2008
Regulation of Adr1 Transcriptional Activator by Phosphorylation
publication
Evidence: moderate
Author Information
Author(s): Kacherovsky Nataly, Tachibana Christine, Amos Emily, Fox David III, Young Elton T.
Primary Institution: Department of Biochemistry, University of Washington, Seattle, Washington, United States of America
Hypothesis
Is phosphorylation of serine 98 on Adr1 involved in regulating its DNA-binding ability?
Conclusion
Phosphorylation of serine 98 on Adr1 is linked to glucose availability and affects its ability to bind DNA.
Supporting Evidence
- Phosphorylation of serine 98 decreases with glucose derepression.
- Mutation of serine 98 affects DNA binding and transcription activation.
- Snf1 kinase is required for Adr1 DNA-binding.
- Adr1 regulates at least 30 glucose-repressed genes.
Takeaway
The study found that a specific part of a protein called Adr1 can change when sugar levels change, which helps the protein do its job better.
Methodology
The study used peptide mapping, western blotting, and chromatin immunoprecipitation to analyze phosphorylation and DNA binding.
Digital Object Identifier (DOI)
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