NMR study of Rcf2 reveals an unusual dimeric topology in detergent micelles.
Related Articles NMR study of Rcf2 reveals an unusual dimeric topology in detergent micelles.
Chembiochem. 2017 Dec 14;:
Authors: Zhou S, Pettersson P, Brzezinski P, Ädelroth P, Mäler L
Abstract
The Saccharomyces (S.) cerevisiae mitochondrial respiratory supercomplex factor 2 (Rcf2) plays a role in assembly of supercomplexes composed of cytochrome bc1 (complex III) and cytochrome c oxidase (complex IV). The Rcf2 protein was here expressed in E. coli, refolded and reconstituted into dodecylphosphocholine (DPC) micelles. The structural properties of Rcf2 were studied by solution NMR and near complete backbone assignment of Rcf2 was achieved. The secondary structure of Rcf2 contains seven helices, of which five are putative transmembrane (TM) helices, including, unexpectedly, a region formed by a charged 20-residue helix at the C-terminus. Further studies demonstrated that Rcf2 forms a dimer and the charged TM helix is involved in this dimer formation. Our results provide a basis for understanding the role of this assembly/regulatory factor in supercomplex formation and function.
PMID: 29240987 [PubMed - as supplied by publisher]
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