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. 2017 Dec 5;16:221. doi: 10.1186/s12934-017-0836-0

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© The Author(s) 2017

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. 2 — Secretion of TRX in NZ9000. a Expression construct for secreted TRX, USP: USP45, PP: propeptide, Linker: flexible linker with TEV cleavage site, His6: HisTag, Term: terminator. b Growth curves for pNZ8148 vector only, USP45-TRX, USP45-PP1-, -PP2-, -PP3-, -PC-TRX. Induction is indicated by a red arrow. c Representative Western blot of cell lysate (C) and secreted (S) fractions. Cell lysate and secreted fractions were concentrated 3 and 25 times respectively and 2 μL of each was loaded onto the gel. The lowest conserved band observed in the cell lysate fraction is a non-specific binding artefact (Additional file 1: Figure S1). % protein yields, with reference to USP45-TRX, and secretion efficiencies of the various TRX constructs are given below. These were calculated based on densitometry and technical triplicates