RESUMO
Biological organisms experience constantly changing environments, from sudden changes in physiology brought about by feeding, to the regular rising and setting of the Sun, to ecological changes over evolutionary timescales. Living organisms have evolved to thrive in this changing world but the general principles by which organisms shape and are shaped by time varying environments remain elusive. Our understanding is particularly poor in the intermediate regime with no separation of timescales, where the environment changes on the same timescale as the physiological or evolutionary response. Experiments to systematically characterize the response to dynamic environments are challenging since such environments are inherently high dimensional. This roadmap deals with the unique role played by time varying environments in biological phenomena across scales, from physiology to evolution, seeking to emphasize the commonalities and the challenges faced in this emerging area of research.
Assuntos
Evolução Biológica , Meio Ambiente , Fenômenos Fisiológicos , Fatores de TempoRESUMO
Many biological regulatory systems respond with a physiological delay when processing signals. A simple model of regulation which respects these features shows how the ability of a delayed output to transmit information is limited: at short times by the time scale of the dynamic input, at long times by that of the dynamic output. We find that topologies of maximally informative networks correspond to commonly occurring biological circuits linked to stress response and that circuits functioning out of steady state may exploit absorbing states to transmit information optimally.
Assuntos
Modelos Biológicos , Animais , Drosophila melanogaster/crescimento & desenvolvimento , Retroalimentação Fisiológica , Probabilidade , Fatores de TempoRESUMO
An exact steady-state solution of the stochastic equations governing the behavior of a gene regulated by a self-generated proteomic atmosphere is presented. The solutions depend on an adiabaticity parameter measuring the relative rate of DNA-protein unbinding and protein degradation. The steady-state solution reveals deviations from the commonly used Ackers et al approximation based on the equilibrium law of mass action, allowing anticooperative behavior in the "nonadiabatic" limit of slow binding and unbinding rates. Noise from binding and unbinding events dominates the shot noise of protein synthesis and degradation up to quite high values of the adiabaticity parameter.