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Biochemistry and biophysics of biological clocks

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Structural, biochemical and biophysical descriptions of clock proteins and their molecular complexes have provided important mechanistic insights into how conformational changes, protein-protein interactions, coenzyme binding, proteasomal degradation, posttranslational modifications, chromatin modifications, and macromolecular (dis)assembly generate and entrain circadian rhythms. High-resolution 3D-structures of mammalian clock proteins and complexes are instrumental for the development of small molecules that target them, both to manipulate clock function and treat clock-associated pathologies. Delineating the molecular and physicochemical interplay of the circadian oscillator with external signals (e.g. light, temperature) and other cellular pathways is vital for understanding the input pathways that allow entrainment to environmental cycles and the output pathways that coordinate a diverse array of rhythmic physiologies important for health.

While insect and mammalian clock components are partially conserved, cyanobacteria, plants and the fungus Neurospora crassa have completely different clock architectures than animals. Structural, biochemical and biophysical studies in these and other clock systems are key to i) elucidating molecular mechanisms that underlie the 24 h phosphorylation timer of the cyanobacterial KaiABC complex, ii) revealing fundamental molecular principles generating rhythmicity in diverse organisms and iii) helping to develop and diversify applications in medicine and agriculture.

We invite research articles and reviews dealing with structural, biochemical and/or biophysical in vitro studies on clock- and clock-related targets, that provide mechanistic insights into their molecular interactions, activities (e.g. light-sensing, enzymatic reactions, cellular transport), functional regulation (e.g. by PTMs, light, pH, temperature, redox changes), and impact on other cellular functions (e.g. integration to cellular metabolism, cell cycle, neuronal firing). We welcome studies on clock proteins involved in biological timing mechanisms of any organism.

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3D CG rendered image of scientifically accurate Bacteriophage HK97 virus capsid Structure based on PDB : 1OHG (ribbon zoomed view)

Editors

  • Eva Wolf, PhD

    Johannes Gutenberg University Mainz, Institute of Molecular Physiology, Germany

  • Masao Doi, PhD

    Kyoto University, Japan

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