Intramolecular competition generates pulsatory protein activity shaped by light, temperature, and evolution.

Area of Science:

• Biochemistry
• Molecular Biology
• Evolutionary Biology

Background:

• Proteins are typically studied at steady state, overlooking their dynamic information processing capabilities.
• Understanding dynamic protein responses is key to deciphering cellular information processing.

Purpose of the Study:

• To investigate dynamic information encoding in individual proteins.
• To elucidate the molecular mechanisms and evolutionary conservation of protein response dynamics.

Main Methods:

• Characterization of the fungal protein BcLOV4's light and temperature responses.
• Analysis of domain interactions and mutational effects on temperature sensing.
• Comparative analysis of homologous proteins across diverse fungal species.

Main Results:

• BcLOV4 exhibits pulsatory responses to light and temperature, adapting to environmental cues.
• Competitive interactions between light- and temperature-sensing domains drive response adaptation.
• Temperature sensing is modular and tunable via mutations in co-evolved loops.
• Photo-thermal response dynamics are conserved in fungal homologues over 300 million years, with adaptations matching host ecological niches.

Conclusions:

• Proteins can dynamically encode environmental information through time-varying activation.
• Molecular principles of dynamic protein activation involve domain competition and modular sensing.
• Conserved, ecologically adapted pulsatory protein activity suggests functional importance for light- and temperature-conditioned responses.