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Role for Protein Kinase A in the Neurospora Circadian Clock by Regulating White Collar-Independent frequency Transcription through Phosphorylation of RCM-1
Protein Kinase A may control the Neurospora circadian clock by modifying frequency gene activity independent of White Collar
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Abstract
Elevated protein kinase A (PKA) activity results in loss of clock function and WC-independent transcription of the frq gene.
- Clock gene expression is regulated by rhythmic activation and repression mechanisms.
- The White Collar (WC) complex activates frq gene transcription, while the FRQ-FRH complex suppresses it.
- RCM-1 is identified as a crucial protein that suppresses WC-independent frq transcription.
- RCM-1 is a phosphoprotein and a substrate of PKA, indicating its role in clock regulation.
- Mutations in PKA phosphorylation sites on RCM-1 lead to uncontrolled frq transcription and disrupted clock function.
- RCM-1 associates with the chromatin at the frq locus, and this association is inhibited by PKA activity.
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