Category:Team Rubby ducky

Figure 3B - Sequence alignment of known phosphorelay proteins shows the His58 of LuxU is highly conserved

Figure 2: LuxO point mutations at Asp-47 resulting in a non-phosphorylated protein mimic causes constitutive luminescence. LuxO point mutations at Asp-47 resulting in a phosphorylated protein mimic causes nearly no light production.

Figure 2: LuxO point mutations at Asp-47 resulting in a non-phosphorylated protein mimic causes constitutive luminescence. LuxO point mutations at Asp-47 resulting in a phosphorylated protein mimic causes nearly no light production.

Figure 6-Thin layer chromatography: Shows the 34K protein transfers acyl groups to both water and beta-mercaptoethanol to produce free fatty acid and acyl-S-mercaptoethanol, respectively.

Chromosomal mutants of V. fischeri prove show that AinS is required for the synthesis for AI-2.

A change in the AinR mutation decreased luminescence which indicates that there may be a distinct regulatory mechanism for AinR.

Figure 1 shows the AinS signaling cascade that controls the Lux operon.

Figure 2A - Shows that when LuxP is mutated to cause it to be mislocalized, strains produce only very low levels of bioluminescence even at a high cell density/high AI-2 concentrations. This indicate that LuxQ remains in its kinase (low cell density) state and is intrinsically a kinase.

Fig. 1 & Fig. 6. LuxP is a AI-2 periplasmic receptor. It works along with LuxQ in quorum sensing.

Figure 2C - Thin layer chromatography. Shows that when the protein of interest is incubated with radiolabeled tetradecanoyl-CoA (an intermediate in fatty acid metabolism) and NADPH, an aldehyde product is produced and low amounts of free fatty acids are detected. This indicates that the Acyl-CoA reductase reduces the tetradecanoyl-CoA intermediate to the aldehyde substrate.