When lowering temperature, the in vivo circadian clock in cyanobacteria follows and surpasses the in vitro protein clock trough the Hopf bifurcation

Sci Rep. 2025 Apr 28;15(1):14884. doi: 10.1038/s41598-025-97412-6.

Abstract

The in vivo circadian clock in single cyanobacteria is studied here by time-lapse fluorescence microscopy when the temperature is lowered below 25°C. We first disentangle the circadian clock behavior from the bacterial cold shock response by identifying a sequence of "death steps" based on cellular indicators. By analyzing only "alive" traces, we show that the dynamic response of individual oscillatory traces to a step-down temperature signal is described by a simple Stuart-Landau oscillator model. The same dynamical analysis applied to in vitro data (KaiC phosphorylation level following a temperature step-down) allows for extracting and comparing both clock's responses to a temperature step down. It appears, therefore, that both oscillators go through a similar supercritical Hopf bifurcation. Finally, to quantitatively describe the temperature dependence of the resulting in vivo and in vitro Stuart-Landau parameters [Formula: see text] and [Formula: see text], we propose two simplified analytical models: temperature-dependent positive feedback or time-delayed negative feedback that is temperature compensated. Our results provide strong constraints for future models by revealing a specific time scale for transitory regimes in the cyanobacterial circadian system and its temperature dependence.

MeSH terms

  • Bacterial Proteins* / metabolism
  • Circadian Clocks* / physiology
  • Circadian Rhythm
  • Circadian Rhythm Signaling Peptides and Proteins / metabolism
  • Cold Temperature
  • Cyanobacteria* / physiology
  • Models, Biological
  • Phosphorylation
  • Temperature

Substances

  • Bacterial Proteins
  • Circadian Rhythm Signaling Peptides and Proteins
  • KaiC protein, cyanobacteria