SNARE-fusion mediated insertion of membrane proteins into native and artificial membranes

Nordlund, Gustav; Brzezinski, Peter; von Ballmoos, Christoph (2014). SNARE-fusion mediated insertion of membrane proteins into native and artificial membranes. Nature communications, 5(1) Nature Publishing Group 10.1038/ncomms5303

[img] Text
ncomms5303.pdf - Published Version
Restricted to registered users only
Available under License Publisher holds Copyright.

Download (421kB)

Membrane proteins carry out functions such as nutrient uptake, ATP synthesis or transmembrane signal transduction. An increasing number of reports indicate that cellular processes are underpinned by regulated interactions between these proteins. Consequently, functional studies of these networks at a molecular level require co-reconstitution of the interacting components. Here, we report a SNARE protein-based method for incorporation of multiple membrane proteins into artificial membrane vesicles of well-defined composition, and for delivery of large water-soluble substrates into these vesicles. The approach is used for in vitro reconstruction of a fully functional bacterial respiratory chain from purified components. Furthermore, the method is used for functional incorporation of the entire F1F0 ATP synthase complex into native bacterial membranes from which this component had been genetically removed. The novel methodology offers a tool to investigate complex interaction networks between membrane-bound proteins at a molecular level, which is expected to generate functional insights into key cellular functions.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)

UniBE Contributor:

von Ballmoos, Christoph

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

2041-1723

Publisher:

Nature Publishing Group

Language:

English

Submitter:

Christoph von Ballmoos

Date Deposited:

26 Mar 2015 09:40

Last Modified:

05 Dec 2022 14:44

Publisher DOI:

10.1038/ncomms5303

BORIS DOI:

10.7892/boris.65895

URI:

https://boris.unibe.ch/id/eprint/65895

Actions (login required)

Edit item Edit item
Provide Feedback