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. 2018 Dec 26;17:200. doi: 10.1186/s12934-018-1048-y

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© The Author(s) 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — Reaction of OhsR-SOH with MSH but alkylation of OhsR with PEG-maleimide. a 20 μM reduced or OhsR-SOH was incubated with or without 200 μM MSH. Proteins were precipitated with TCA, treated with 5 mM PEG-maleimide, and evaluated on a CBB-stained 15% SDS-PAGE. b Proteins (50 μM) treated with 50 mM DTT were further incubated with or without 750 μM MSH, 250 μM CHP, or 250 μM CHP and 750 μM MSH, and samples were then separated by 15% nonreducing SDS-PAGE. c Analysis of sulfonic acid formed on OhsR by MALDI-TOF-TOF MS/MS. Bands (labeled (c)) excised from nonreducing gels in b were treated with trypsin and subjected to MS analysis. Only the relevant portion of each mass spectrum is shown