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. 2016 May 12;7:716. doi: 10.3389/fmicb.2016.00716

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Copyright © 2016 Long, Xu, Qian, Zhang and Lu.

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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Three conserved histidine residues in MrsA are required for the response to oxidative and azole stresses. (A) Schematic view of the MrsA point mutation. The His residues (H) of MrsA located at positions 38 (H1), 96 (H2), and 214 (H5) and a glycine residue (G) located at position 60 (H1) were mutated to alanine (A). The glycine residue was mutated as a control. (B) Conidia of each strain were serially diluted and spotted onto YAG plates in the presence of 300 μM BPS, 10 mM Fe (FeCl₃), 3 mM H₂O₂, 25 μM menadione and 0.75 μg ml^-1 ITZ.