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Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation
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: 102018 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 115, no 12, p. 3048-3053Article in journal (Refereed) Published
Abstract [en]

The Saccharomyces cerevisiae respiratory supercomplex factor 1 (Rcf1) protein is located in the mitochondrial inner membrane where it is involved in formation of supercomplexes composed of respiratory complexes III and IV. We report the solution structure of Rcf1, which forms a dimer in dodecylphosphocholine (DPC) micelles, where each monomer consists of a bundle of five transmembrane (TM) helices and a short flexible soluble helix (SH). Three TM helices are unusually charged and provide the dimerization interface consisting of 10 putative salt bridges, defining a charge zipper motif. The dimer structure is supported by molecular dynamics (MD) simulations in DPC, although the simulations show a more dynamic dimer interface than the NMR data. Furthermore, CD and NMR data indicate that Rcf1 undergoes a structural change when reconstituted in liposomes, which is supported by MD data, suggesting that the dimer structure is unstable in a planar membrane environment. Collectively, these data indicate a dynamic monomer-dimer equilibrium. Furthermore, the Rcf1 dimer interacts with cytochrome c, suggesting a role as an electron-transfer bridge between complexes III and IV. The Rcf1 structure will help in understanding its functional roles at a molecular level.

Place, publisher, year, edition, pages
2018. Vol. 115, no 12, p. 3048-3053
Keywords [en]
charge zipper, membrane proteins, mitochondria, bicelles, lipids
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-154705DOI: 10.1073/pnas.1712061115ISI: 000427829500069PubMedID: 29507228OAI: oai:DiVA.org:su-154705DiVA, id: diva2:1197255
Available from: 2018-04-12 Created: 2018-04-12 Last updated: 2018-04-12Bibliographically approved

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Zhou, ShuPettersson, PontusSjöholm, JohannesSjöstrand, DanHögbom, MartinBrzezinski, PeterMäler, LenaÄdelroth, Pia
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