Yao Xu

TL;DR: It is shown that oxidation–reduction cycles of peroxiredoxin proteins constitute a universal marker for circadian rhythms in all domains of life, by characterizing their oscillations in a variety of model organisms and exploring the interconnectivity between these metabolic cycles and transcription–translation feedback loops of the clockwork in each system.

TL;DR: The BRET technique is used to demonstrate that the clock protein KaiB interacts to form homodimers, and should be particularly useful for testing protein interactions within native cells, especially with integral membrane proteins or proteins targeted to specific organelles.

TL;DR: It is concluded that the circadian period in cyanobacteria is determined by the phosphorylation status of KaiC and also by the degradation rate of Kai C, which is integrated into a model proposing rhythmic changes in chromosomal status.

TL;DR: The crystal structure of KaiC reveals ATP binding, inter-subunit organization, a scaffold for Kai-protein complex formation, the location of critical KaiC mutations, and evolutionary relationships to other proteins.

TL;DR: This work shows that in the cyanobacterium Synechococcus elongate, non-optimal codon usage was selected as a post-transcriptional mechanism to switch between circadian and non-circadian regulation of gene expression as an adaptive response to environmental conditions, and challenges the long-standing view of directional selection towards optimal codons.