Fig. 3: NanR dimers assemble on the (GGTATA)3-repeat operator. | Nature Communications

Fig. 3: NanR dimers assemble on the (GGTATA)3-repeat operator.

From: Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism

Fig. 3: NanR dimers assemble on the (GGTATA)3-repeat operator.The alternative text for this image may have been generated using AI.

a Sedimentation coefficient distributions of the NanR (blue) and the (GGTATA)3-repeat DNA operator (black) controls, measured individually at 280 and 260 nm, respectively. be Deconvoluted sedimentation coefficient distributions resulting from the titration of NanR into (GGTATA)3-repeat DNA (0.5 µM): 0.5 µM NanR (b), 1.5 µM NanR (c), 3.0 µM NanR (d), and 5.0 µM NanR (e). A shift in the sedimentation coefficient is observed with increasing NanR concentration, consistent with hetero-complex formation. The molar ratio of the integrated peaks (shaded in gray) and the oligomeric state of each hetero-complex is shown. The presence of excess protein free of any co-migrating DNA in e indicates that hetero-complex formation has reached saturation. All plots are presented as g(s) distributions with the molar concentration for each interacting partner (protein and DNA) plotted on the y-axis. Hydrodynamic parameters are in Supplementary Table 5.

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