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. 2016 Oct 21;7:1654. doi: 10.3389/fmicb.2016.01654

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Copyright © 2016 Venkatesan, Palaniyandi, Sharma, Bisht and Narayanan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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PknI interacts with Rv2159c. (A,B) Pull down assay confirms the interaction between PknI and Rv2159c. Cytoplasmic crude lysates containing recombinant His-PknI and GST-Rv2159c proteins were incubated with Ni-NTA resin (A, lane 1) or glutathione sepharose resin respectively (B, lane 1). Unbound proteins (lane 2) were washed off and incubated with their respective substrates. The protein complexes were eluted (lane 3) and immunoblotted with anti-GST (A) and anti-His antibodies (B) respectively. As a control, the bait proteins were incubated with bovine serum albumin (BSA) protein (lane 4). Lane 1 from (A) and (B) shows the bait protein load controls of PknI and Rv2159c proteins that are probed against anti-His (A) and anti-GST (B) antibodies respectively. Several lanes were merged for photogenic purpose. (C) FWB identifies the crucial amino acids in PknI-Rv2159c interaction. The purified GST-Rv2159c point mutants A49P (lane 1), G50A (lane 2), W51A (lane 3) and 49AGW51 (lane 4) along with purified Rv2159c protein (lane 5) were incubated with His-PknI protein and subsequently probed with anti-His antibody. Lane M, Molecular mass standard.