NMR Study of Rcf2 Reveals an Unusual Dimeric Topology in Detergent Micelles. (25th January 2018)

• Record Type: Journal Article
• Authors: Zhou, Shu; Pettersson, Pontus; Brzezinski, Peter; Ädelroth, Pia; Mäler, Lena
• Is Part Of: Chembiochem. Volume 19:Number 5(2018)
• Page Start: 444
• Page End: 447
• Publication Date: 2018-01-25
• Subjects: dimers -- membrane protein -- membrane topology -- NMR spectroscopy -- respiratory supercomplex factor; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201700664
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: The Saccharomyces cerevisiae mitochondrial respiratory supercomplex factor 2 (Rcf2) plays a role in assembly of supercomplexes composed of cytochrome bc 1 (complex III ) and cytochrome c oxidase (complex IV ). We expressed the Rcf2 protein in Escherichia coli, refolded it, and reconstituted it 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. Abstract : Super formation of supercomplexes : The S. cerevisiae mitochondrial respiratory supercomplex factor 2 (Rcf2) plays a role in respiratory supercomplex assembly. Solution NMR spectroscopy demonstrated that the Rcf2 dimer contains seven helices, with five being putative transmembrane helices, including a charged helix involved in dimer formation. This provides a basis for understanding the role of Rcf2 in supercomplex formation and function.