Just out - photoreceptors: We've examined the generality of the LOV (Light-Oxygen-Voltage) signaling model we first reported for the phototropin / AsLOV2 system (Harper et al. 2003, Freddolino et al. 2013). An analogous mechanism used is by EL222, a bacterial LOV-HTH DNA-binding protein (Nash et al. 2011). Inactive in the dark, EL222 undergoes light-dependent structural changes to bind DNA sites identified by genomic and selection methods (Rivera-Cancel et al. 2012, Zoltowski et al. 2013) to activate gene transcription in vivo. Recent engineering work from our group has extended the generality of this system to work in eukaryotic cells as well (Motta-Mena et al. 2014). Parallel studies on LOV-histidine kinases from E. litoralis (Corrêa et al., 2013) have uncovered regulatory mechanisms and downstream partners, revealing a stress response pathway conserved among bacteria.

Just out - bHLH/PAS: We've reported two approaches to regulate the HIF transcription factors with small molecules in living cells. One route exploits a large cavity within the HIF-2α PAS-B domain (Scheuermann et al. 2009, Key et al. 2009), providing a site for high-affinity ligands to trigger allosteric changes that disrupt HIF-2α/ARNT complexes (Scheuermann et al., 2013, Rogers et al., 2013). Another strategy targets all HIF isoforms (Guo et al. 2013) by disrupting interactions between the ARNT subunit and CCC coactivator proteins, including TACC3 (Partch and Gardner 2011).

for April 23, 2014, as found in X Han et al., Science 314(2006): 109:

"The apparent 'ball of spaghetti' tertiary structure (of the protein) only allows for leavages in its unraveled ends, with >800 central residues untouched despite these multiple activations."