Figure 6. The C-terminal domain interacts with the SSB-Ct.

(A) SSB-Ct binding pocket. SSB-Ct is shown as stick. The electron density of SSB-Ct is shown in blue with the refined 2Fo-Fc map contoured at 1σ. (B) Interactions of the SSB-Ct and C-terminal domain. Both SSB-Ct (yellow) and residues involved in SSB-Ct interactions (green) are shown as sticks. The ionic bond between the Asp298 of SSB-Ct and Lys629 of drRecJ is indicated by a yellow dashed line. (C) SSB enhances wild-type drRecJ degradation. Y575A mutant drRecJ (RecJ₅₇₅), wild-type drSSB (SSB_WT) and drSSB lacking eight C-terminal residues (SSB_ΔC) were purified to perform the nuclease assays. For the reaction, DNA with a 3´-ssDNA overhang was pre-incubated with 200 nM SSB_WT or SSB_ΔC and treated with drRecJ or RecJ₅₇₅ (5 and 20 nM) (see Materials and methods).

DOI: http://dx.doi.org/10.7554/eLife.14294.019

Figure 6—figure supplement 1. SSB enhances wild-type drRecJ degradation on ssDNA.

Y575A mutant drRecJ (RecJ₅₇₅), wild-type drSSB (SSB_WT) and drSSB lacking eight C-terminal residues (SSB_ΔC) were purified to perform the nuclease assays. For the reaction, 100 nM ssDNA was pre-incubated with 200 nM SSB_WT or SSB_ΔC and treated with drRecJ or RecJ₅₇₅ (2.5 and 5 nM, or 10 and 20 nM) (see Materials and methods).

DOI: http://dx.doi.org/10.7554/eLife.14294.020

Figure 6—figure supplement 2. Structural comparison of the SSB-Ct binding pockets of RecJ, Rnase HI (4Z0U), RecO (3Q8D) and Pol III (3SXU).

The SSB-Ct are shown as sticks and colored in yellow. Residues interact with SSB-Ct are labeled, shown as sticks and colored in green.

DOI: http://dx.doi.org/10.7554/eLife.14294.021