Fusion Domains Guide the Oriented Insertion of Light-Driven Proton Pumps into Liposomes.

Ritzmann, Noah; Thoma, Johannes; Hirschi, Stephan; Kalbermatter, David; Fotiadis, Dimitrios José; Müller, Daniel J (2017). Fusion Domains Guide the Oriented Insertion of Light-Driven Proton Pumps into Liposomes. Biophysical journal, 113(6), pp. 1181-1186. Biophysical Society 10.1016/j.bpj.2017.06.022

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One major objective of synthetic biology is the bottom-up assembly of minimalistic nanocells consisting of lipid or polymer vesicles as architectural scaffolds and of membrane and soluble proteins as functional elements. However, there is no reliable method to orient membrane proteins reconstituted into vesicles. Here, we introduce a simple approach to orient the insertion of the light-driven proton pump proteorhodopsin (PR) into liposomes. To this end, we engineered red or green fluorescent proteins to the N- or C-terminus of PR, respectively. The fluorescent proteins optically identified the PR constructs and guided the insertion of PR into liposomes with the unoccupied terminal end facing inward. Using the PR constructs, we generated proton gradients across the vesicle membrane along predefined directions such as are required to power (bio)chemical processes in nanocells. Our approach may be adapted to direct the insertion of other membrane proteins into vesicles.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Hirschi, Stephan; Kalbermatter, David and Fotiadis, Dimitrios José

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

0006-3495

Publisher:

Biophysical Society

Language:

English

Submitter:

Barbara Järmann-Bangerter

Date Deposited:

22 Mar 2018 09:27

Last Modified:

22 Mar 2018 09:27

Publisher DOI:

10.1016/j.bpj.2017.06.022

PubMed ID:

28697898

BORIS DOI:

10.7892/boris.111349

URI:

https://boris.unibe.ch/id/eprint/111349

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