Fig. 3: Analysis of DmREDusk and DrREDusk variants with modified linkers.
From: Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling
a Bacteria harboring different DmREDusk (left) and DrREDusk (right) systems were incubated under red light (red bars) or in darkness (gray). The DsRed reporter fluorescence was determined as the mean ± s.d. of n = 3 biologically independent replicates and compared to that of DmREDusk, DrREDusk (both denoted 'Ref' and labeled with †), and of controls lacking the fluorescent protein but containing a multiple-cloning site (MCS) instead. The relative length of the linker connecting the photosensory module (PSM) and the effector moiety of the SHK variants is indicated on the abscissa. Variants with identical linker lengths but different sequences are designated with the suffixes ‘a’ and ‘b’. The actual linker sequences are provided in Suppl. Fig. 7b. b Distribution of relative linker lengths of DmREDusk variants (top panel), with red-light-repressed (termed ‘Ref-like’) and inverted, red-light-activated specimens (termed ‘Inverted’) shown as black and white bars, respectively. The dagger symbol (†) denotes the linker length in DmF1 that underlies the original DmREDusk. The bottom panel shows in comparison the linkers in naturally occurring BphP SHKs. Separate analyses consider all histidine-kinase families (blue) or only HWE SHKs (cyan). c Analysis of the linker lengths in panel b according to their heptad coiled-coil register. To this end, the distribution is plotted against the remainder after division by seven of the linker length (that is, the modulo 7). Color codes as in panel b. Source data are provided as a Source Data file.
