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

Cellulase Fusion proteins Outer membrane cytochromes Protein export Shewanella oneidensis Type II secretion system

Journal

Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812

Informations de publication

Date de publication:
23 Dec 2019
Historique:
received: 21 10 2019
accepted: 13 12 2019
entrez: 25 12 2019
pubmed: 25 12 2019
medline: 16 4 2020
Statut: epublish

Résumé

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.

Identifiants

pubmed: 31870378
doi: 10.1186/s12934-019-1270-2
pii: 10.1186/s12934-019-1270-2
pmc: PMC6929479
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
Cytochromes 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

216

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Auteurs

Helge M Dietrich (HM)

Department of Molecular Microbiology and Bioenergetics, Goethe University, Frankfurt, Germany.

Miriam Edel (M)

Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.

Thea Bursac (T)

Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.

Manfred Meier (M)

Institute for Biological Interfaces, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany.

Katrin Sturm-Richter (K)

Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.

Johannes Gescher (J)

Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany. johannes.gescher@kit.edu.
Institute for Biological Interfaces, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany. johannes.gescher@kit.edu.

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Classifications MeSH