Dietrich, Helge M.Helge M.DietrichEdel, MiriamMiriamEdelBursać, Thea ViolaThea ViolaBursaćMeier, ManfredManfredMeierSturm-Richter, KatrinKatrinSturm-RichterGescher, JohannesJohannesGescher2021-08-312021-08-312019-12-23Microbial Cell Factories 18 (1): 216 (2019-12-23)http://hdl.handle.net/11420/10227This study reveals that it is possible to secrete truncated versions of outer membrane cytochromes into the culture supernatant and that these proteins can provide a basis for the export of heterologously produced proteins. Different soluble and truncated versions of the outer membrane cytochrome MtrF were analyzed for their suitability to be secreted. A protein version with a very short truncation of the N-terminus to remove the recognition sequence for the addition of a lipid anchor is secreted efficiently to the culture supernatant, and moreover this protein could be further truncated by a deletion of 160 amino acid and still is detectable in the supernatant. By coupling a cellulase to this soluble outer membrane cytochrome, the export efficiency was measured by means of relative cellulase activity. We conclude that outer membrane cytochromes of S. oneidensis can be applied as transporters for the export of target proteins into the medium using the type II secretion pathway.en1475-285920191https://creativecommons.org/licenses/by/4.0/CellulaseFusion proteinsOuter membrane cytochromesProtein exportShewanella oneidensisType II secretion systemBiowissenschaften, BiologieJournal Article10.15480/882.374810.1186/s12934-019-1270-210.15480/882.374831870378Journal Article