NMR Study of Rcf2 Reveals an Unusual Dimeric Topology in Detergent Micelles

Zhou, Shu; Pettersson, Per; Brzezinski, Peter; Ädelroth, Pia; Mäler, Lena

doi:10.1002/cbic.201700664

Cited by 5 publications

(13 citation statements)

References 34 publications

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“…A short helix, SH1 (E90-K100), is situated between TM2 and TM3, and a second short helix with no well-defined location, SH2 (V211-F222), is positioned at the C terminus. The overall topology of the present structure is in excellent agreement with the results from our earlier study using PREs (Zhou et al, 2018a).…”

Section: Solution Structure Of the Rcf2 Dimer In Dpc Micellessupporting

confidence: 91%

“…Article good approximation for the dimensions and chemical environment of a membrane bilayer (White and Wimley, 1999). The observed NOE contacts between Rcf2 and DPC are consistent with our previously reported results from PRE and hydrogendeuterium exchange experiments (Zhou et al, 2018a), which demonstrated that the charged TM5 is buried in DPC micelles.…”

Section: Ll Open Accesssupporting

confidence: 90%

“…Residue types are color coded with the hydrophobic residues (I, L, V, A, M, G, F, W, and P) in gray, hydrophilic residues (S, C, Y, N, Q, and T) in green, and positively (R, K, and H) and negatively charged (D and E) residues in blue and red, respectively. Dashed horizontal lines indicate the suggested membrane boundaries based on previously published data (Zhou et al, 2018a).…”

Section: Solution Structure Of the Rcf2 Dimer In Dpc Micellesmentioning

confidence: 98%

“…We have previously reported that Rcf2 forms a stable dimer in DPC micelles, with seven helical segments in each monomer (Zhou et al, 2018a). The overall topology of Rcf2, with two solu-ble and five putative TM helices in each monomer as well as the location of the dimer interface (Figure 1) was determined using paramagnetic relaxation enhancement (PRE) experiments with water-soluble gadodiamide and detergent-soluble 16-doxylstearic acid.…”

Section: Nmr Resonance Assignment and Structural Restraintsmentioning

confidence: 99%

“…Understanding the role of Rcf2 in respiratory complex and supercomplex formation is dependent on knowledge of its structure, which is unknown and neither Rcf1 nor Rcf2 were observed in the recent cryo-EM structures of yeast supercomplexes (Hartley et al, 2019;Rathore et al, 2019, but see Hartley et al, 2020, andDiscussion). We have previously reported that Rcf2 purified from E. coli can form a dimer in dodecylphosphocholine (DPC) micelles where each Rcf2 monomer contains two flexible short helices (SHs) and five putative TM helices, including an unexpected charged helix at the C terminus, which is involved in dimer formation (Zhou et al, 2018a).…”

Section: Introductionmentioning

confidence: 99%

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NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2

et al. 2021

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Section: Solution Structure Of the Rcf2 Dimer In Dpc Micellessupporting

confidence: 91%

Section: Ll Open Accesssupporting

confidence: 90%

Section: Solution Structure Of the Rcf2 Dimer In Dpc Micellesmentioning

confidence: 98%

Section: Nmr Resonance Assignment and Structural Restraintsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2

et al. 2021

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Structure and Mechanism of Respiratory III–IV Supercomplexes in Bioenergetic Membranes

2021

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In the final steps of energy conservation in aerobic organisms, free energy from electron transfer through the respiratory chain is transduced into a proton electrochemical gradient across a membrane. In mitochondria and many bacteria, reduction of the dioxygen electron acceptor is catalyzed by cytochrome c oxidase (complex IV), which receives electrons from cytochrome bc 1 (complex III), via membrane-bound or watersoluble cytochrome c. These complexes function independently, but in many organisms they associate to form supercomplexes. Here, we review the structural features and the functional significance of the nonobligate III 2 IV 1/2 Saccharomyces cerevisiae mitochondrial supercomplex as well as the obligate III 2 IV 2 supercomplex from actinobacteria. The analysis is centered around the Q-cycle of complex III, proton uptake by CytcO, as well as mechanistic and structural solutions to the electronic link between complexes III and IV. CONTENTS 1. Introduction 9645 2. Complex III 9648 2.1. Catalytic Reaction and Quinone Binding 9649 2.2. The Bifurcated Electron Transfer 9650 2.2.1. Canonical Complex III 9650 2.2.2. M. smegmatis and C. glutamicum Supercomplexes 9651 2.3. Proton Release from the Q P Site 9651 2.3.1. Canonical Complex III 9651 2.3.2. M. smegmatis and C. glutamicum Supercomplexes 9651 3. Complex IV 9652 3.1. The Core Subunits 9653 3.2. The Catalytic Reaction and Proton Pathways 9653 3.3. Peripheral subunits of the S. cerevisiae CytcO 9654 3.4. The M. smegmatis CytcO 9654 3.5. Nonredox Active Metal Sites 9655 3.6. The Putative CytcO Dimer 9655 4. Complex III−IV Supercomplexes 9656 4.1. The S. cerevisiae Supercomplex 9656 4.2. Other (I)III 2 IV 1/2 Supercomplexes 9656 4.3. Cardiolipin in Supercomplexes 9657 4.4. Respiratory Supercomplex Factors 9658 4.5. Superoxide Dismutase in the M. smegmatis Supercomplex 9658 5. Interaction of Complexes III 2 and IV with Cytochrome c 9659 5.1. Cyt. c Binding to Complexes III and IV 9659 5.2. The Electronic Link between Complexes III and IV 5.2.1. Diffusion in 3D 5.2.2. Diffusion in 2D 5.2.3. Effects of Cox5/cyt. c Isoforms 5.2.4. Binding of cyt. c to Rcf1 6. Why Supercomplexes? 6.1. Changes in Structure or Activity upon Formation of Supercomplexes 6.2. Protein Distribution and Aggregation 6.3. Production of ROS 6.4. Free Energy Conservation 6.5. The Redox State and Binding of cyt. c

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Cryo-EM structure and function of S. pombe complex IV with bound respiratory supercomplex factor

et al. 2023

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Fission yeast Schizosaccharomyces pombe serves as model organism for studying higher eukaryotes. We combined the use of cryo-EM and spectroscopy to investigate the structure and function of affinity purified respiratory complex IV (CIV) from S. pombe. The reaction sequence of the reduced enzyme with O2 proceeds over a time scale of µs-ms, similar to that of the mammalian CIV. The cryo-EM structure of CIV revealed eleven subunits as well as a bound hypoxia-induced gene 1 (Hig1) domain of respiratory supercomplex factor 2 (Rcf2). These results suggest that binding of Rcf2 does not require the presence of a CIII-CIV supercomplex, i.e. Rcf2 is a component of CIV. An AlphaFold-Multimer model suggests that the Hig1 domains of both Rcf1 and Rcf2 bind at the same site of CIV suggesting that their binding is mutually exclusive. Furthermore, the differential functional effect of Rcf1 or Rcf2 is presumably caused by interactions of CIV with their different non-Hig1 domain parts.

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NMR Study of Rcf2 Reveals an Unusual Dimeric Topology in Detergent Micelles

Cited by 5 publications

References 34 publications

NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2

NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2

Structure and Mechanism of Respiratory III–IV Supercomplexes in Bioenergetic Membranes

Cryo-EM structure and function of S. pombe complex IV with bound respiratory supercomplex factor

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