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. 2018 Nov 21;9:2837. doi: 10.3389/fmicb.2018.02837

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Copyright © 2018 Dragomirova, Rothe, Schwoch, Hartwig, Pinske and Sawers.

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) and the copyright owner(s) 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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HupX is not required for heterologous HupSL activity. (A) Schematic representation of the plasmids used in this study is shown. The plasmid inserts are not drawn to scale but the complete hupXSLhoxM region encompasses 4216 bp (Hartwig et al., 2015b). (B) An in-gel activity stain for hydrogen-oxidizing activity is shown. Crude extracts (70 μg of protein; 30 μg in the case of wild type MC4100) derived from FTD147 (ΔhyaB ΔhybC ΔhycE) carrying the indicated plasmids were applied to a native polyacrylamide gel (7.5% w/v polyacrylamide). The migration positions of HupSL and the E. coli hydrogenases are indicated. The formate dehydrogenases Fdh-N and Fdh-O (Fdh-N/O) have a weak hydrogen-oxidizing activity (Soboh et al., 2011), which is also indicated and was used as an internal loading control for the experiment.