In the plant circadian clock photoreceptor ZEITLUPE, evolutionarily selected residues distinguish photocycle kinetics and allosteric signal transduction pathways to permit proper circadian timing.
Light absorption by the algal transcription factor Aureochrome 1a causes dimerization at the light-oxygen-voltage (LOV) sensing domain, which has implications for the design of synthetic photoreceptors for optogenetics.
SPARK2 allows a transcriptional readout of inter- and intracellular protein-protein interactions, with near-zero background, by employing proximity-dependent luciferase-LOV regulation.
A light-dependent two-hybrid tool with transcriptional readout detects multiple protein-protein interactions in living mammalian cells with high signal-to-background ratios and enables genetic selections.
Nucleolar protein localization involves the phase separation within the nucleolar matrix via three types of multivalent features: acidic tracts, nucleic acid binding domains and arginine-rich low complexity sequences.
The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.
