Circadian rhythmicity by autocatalysis
2006

Circadian Rhythmicity by Autocatalysis

publication Evidence: moderate

Author Information

Author(s): Mehra Arun, Hong Christian I, Shi Mi, Loros Jennifer J, Dunlap Jay C, Ruoff Peter

Primary Institution: Dartmouth Medical School

Hypothesis

The study proposes a model where the autocatalytic phosphorylation and dephosphorylation of KaiC proteins are the source of circadian rhythmicity.

Conclusion

The model successfully explains temperature-compensated circadian oscillations in KaiC phosphorylation based on autocatalysis.

Supporting Evidence

  • The model predicts that the period length and the ratio of phosphorylated to unphosphorylated KaiC are linked to the stability of the ternary complex formed by the Kai proteins.
  • The study demonstrates that the KaiC oscillator can be reconstituted in vitro, showing temperature compensation.
  • The model suggests that autocatalysis is essential for sustained oscillations in the KaiC phosphorylation rhythm.

Takeaway

This study shows how a simple system of proteins can create a biological clock that keeps time, even when the temperature changes.

Methodology

The study developed a deterministic model based on known interactions and phosphorylation events among Kai proteins.

Limitations

The model's complexity may not capture all biological nuances, and some rate constants are not well-defined.

Digital Object Identifier (DOI)

10.1371/journal.pcbi.0020096

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