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Lipid-mediated Protein-protein Interactions Modulate Respiration-driven ATP Synthesis
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 6
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 24113Article in journal (Refereed) Published
Abstract [en]

Energy conversion in biological systems is underpinned by membrane-bound proton transporters that generate and maintain a proton electrochemical gradient across the membrane which used, e.g. for generation of ATP by the ATP synthase. Here, we have co-reconstituted the proton pump cytochrome bo3 (ubiquinol oxidase) together with ATP synthase in liposomes and studied the effect of changing the lipid composition on the ATP synthesis activity driven by proton pumping. We found that for 100 nm liposomes, containing 5 of each proteins, the ATP synthesis rates decreased significantly with increasing fractions of DOPA, DOPE, DOPG or cardiolipin added to liposomes made of DOPC; with e.g. 5% DOPG, we observed an almost 50% decrease in the ATP synthesis rate. However, upon increasing the average distance between the proton pumps and ATP synthases, the ATP synthesis rate dropped and the lipid dependence of this activity vanished. The data indicate that protons are transferred along the membrane, between cytochrome bo3 and the ATP synthase, but only at sufficiently high protein densities. We also argue that the local protein density may be modulated by lipid-dependent changes in interactions between the two proteins complexes, which points to a mechanism by which the cell may regulate the overall activity of the respiratory chain.

Place, publisher, year, edition, pages
2016. Vol. 6, 24113
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Biological Sciences
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URN: urn:nbn:se:su:diva-130172DOI: 10.1038/srep24113ISI: 000374219300001PubMedID: 27063297OAI: oai:DiVA.org:su-130172DiVA: diva2:927151
Available from: 2016-05-11 Created: 2016-05-09 Last updated: 2016-05-11Bibliographically approved

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Nilsson, TobiasRydström Lundin, CamillaÄdelroth, Piavon Ballmoos, ChristophBrzezinski, Peter
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