Fig. 4: S. aureus σA1.1 suppresses the DNA binding activity of free σA and σA-RNAP holoenzyme. | Nature Communications

Fig. 4: S. aureus σA1.1 suppresses the DNA binding activity of free σA and σA-RNAP holoenzyme.

From: Structural basis of promoter recognition by Staphylococcus aureus RNA polymerase

Fig. 4

A Structural comparison of S. aureus σA1.1, E. coli σ701.1 (PDB: 4LK1), and B. subtilis σA1.1 (PDB: 5MWW). The structure of S. aureus σA1.1 is predicted by AlphaFold. B Fluorescence polarization assay shows that σA1.1 truncated σA binds promoter DNA better than the full-length σA. Error bars represent mean ± SD of n = 3 experiments. 1.25 μM, p = 0.0027; 2.5 μM, p = 0.0019; 5 μM, p = 0.0008; 10 μM, p = 0.0003. Two-tailed Student’s t test. Source data are provided as a Source Data file. C EMSA shows that truncation of σA1.1 increases σA-dependent RPo formation. Source data are provided as a Source Data file.

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