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. Author manuscript; available in PMC: 2010 Jun 28.
Published in final edited form as: Cell. 2009 May 15;137(4):697–707. doi: 10.1016/j.cell.2009.04.044

Figure 5.

Figure 5

SMC binds Spo0J-coated DNA with higher affinity than free DNA or LacI-coated DNA. Electrophoretic mobility shift analysis of purified Spo0J, Lac Repressor (LacI), and SMC. The DNA substrates were a 461 bp fragment containing a parS site and a 574 bp fragment containing an array of 15 lacO sites. (A) Coomassie-stained gel of the purified proteins. (B) Spo0J and LacI coat their respective DNA substrates. The protein concentrations ranged from 56nM to 1.8 μM with 2-fold step increases. Fully saturated DNA substrates are indicated (carets) (C) SMC has the highest affinity for the Spo0J nucleoprotein complex. The concentration of Spo0J and LacI used to generate the filament substrates were 1.8 μM. The concentrations of SMC were 33 nM, 100 nM, and 300 nM. The super-shifted species containing SMC and Spo0J-parS are indicated (bracket).