Structural basis for the interaction of Escherichia coli NusA with protein N of phage λ

Bonin et al. 10.1073/pnas.0405883101.

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Fig. 4. Electrophoretic gel-mobility shift analyses. (A) (Lanes 1–5) Titration of radiolabeled boxB RNA (50,000 cpm) with increasing amounts (0–10 mM) of l N (residues 1–40). (Lanes 6–9) Titration of a l N(1–40)–boxB complex (50,000 cpm RNA) with increasing amounts (0.25–10 mM) of NusA AR1–AR2. High concentrations of the NusA AR1–AR2 protein can slightly supershift the l N(1–40)–boxB complex. (Lanes 10–13) Titration of radiolabeled boxB RNA (50,000 cpm) with increasing amounts (0–10 m M) of NusA AR1–AR2. No RNA binding to the AR1–AR2 region was detectable in this assay. (B) Titration of nut site RNA (5,000 cpm) with increasing amounts of full-length NusA (0–20 mM) in the absence of lN peptide (lanes 1–6) or in the presence of 100 mM l N (residues 34-47). Binding of NusA to the RNA is weak irrespective of the presence of the peptide.

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