SEARCH

SEARCH BY CITATION

FilenameFormatSizeDescription
febs12208-sup-0001-FigS1-S11_TableS1-S2.zipapplication/ZIP1195K

Fig. S1. Sequence alignment of MtRecG with EcRecG.

Fig. S2. (A) Schematic representation of MtRecG with TEV protease site. (B) Overexpression and purification of MtRecG. (C) Immunoblot of MtRecG at various stages of purification.

Fig. S3. M. tuberculosis recG rescues the sensitivity of E. coli ΔrecG cells to MMS and UV damage.

Fig. S4. DNA-damage-induced expression of M. tuberculosis RecG.

Fig. S5. DNA binding activity of MtRecG to duplex DNA (A) and ssDNA (B). (C) Quantitative analysis of MtRecG DNA binding activity with various DNA substrates.

Fig. S6. Stability of the MtRecG–HJ complex in the presence of an increasing concentration of NaCl.

Fig. S7. DNase I footprinting of MtRecG bound to immobile HJs.

Fig. S8. KMnO4 chemical probing of MtRecG bound to mobile HJs (A) or immobile HJs (B).

Fig. S9. (A) Helicase activity of MtRecG with duplex DNA. (B) Quantitative analysis of MtRecG helicase activity with various DNA substrates.

Fig. S10. D-loop binding (A, B, C, D) and unwinding (E, F, G, H) activity of MtRecG.

Fig. S11. DNA-dependent ATPase activity of MtRecG.

Table S1. Various substrates that were used in this study.

Table S2. Comparison of DNA binding and unwinding activity of MtRecG with various substrates.

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.