These authors contributed equally to this work
Evidence for the role of Mycobacterium tuberculosis RecG helicase in DNA repair and recombination
Article first published online: 21 MAR 2013
© 2013 The Authors Journal compilation © 2013 FEBS
Volume 280, Issue 8, pages 1841–1860, April 2013
How to Cite
Thakur, R. S., Basavaraju, S., Somyajit, K., Jain, A., Subramanya, S., Muniyappa, K. and Nagaraju, G. (2013), Evidence for the role of Mycobacterium tuberculosis RecG helicase in DNA repair and recombination. FEBS Journal, 280: 1841–1860. doi: 10.1111/febs.12208
- Issue published online: 11 APR 2013
- Article first published online: 21 MAR 2013
- Accepted manuscript online: 25 FEB 2013 11:58AM EST
- Manuscript Accepted: 18 FEB 2013
- Manuscript Revised: 5 FEB 2013
- Manuscript Received: 16 NOV 2012
- Department of Atomic Energy. Grant Number: 2010/37B/40/BRNS/1437
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.
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