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. 2010 Aug 19;38(22):8219–8230. doi: 10.1093/nar/gkq737

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — N-terminus of Rv1495 regulates the topoisomerase activities of MtbTopA. Topoisomerase activity and bacterial two-hybrid assays for all mutants were performed as described under ‘Materials and Methods’ section. + represents growth on the screening plate; − represents no growth on the screening plate. (A) The N-terminal mutant fragments of Rv1495 containing 56 and 28 amino acid residues (left panel) and their interactions with MtbTopA assayed by the bacterial two-hybrid system (right panel). (B) Two synthesized short peptides and their amino acid sequences. (C) Effect of different amount of Rv1495-N28, Rv1495-N56, and Rv1495-N(29-56) (0–6.0 μM) on topoisomerase activity.