Soluble versions of outer membrane cytochromes function as exporters for heterologously produced cargo proteins

This 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.

Subjects

Cellulase

Fusion proteins

Outer membrane cytochromes

Protein export

Shewanella oneidensis

Type II secretion system

DDC Class

570: Biowissenschaften, Biologie

Lizenz

https://creativecommons.org/licenses/by/4.0/

Name

s12934-019-1270-2.pdf

Size

1.56 MB

Format

Adobe PDF

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Soluble versions of outer membrane cytochromes function as exporters for heterologously produced cargo proteins