Cox26 is a novel stoichiometric subunit of the yeast cytochrome c oxidase

Levchenko, Maria; Wuttke, Jan-Moritz; Römpler, Katharina; Schmidt, Bernhard; Neifer, Klaus; Juris, Lisa; Wissel, Mirjam; Rehling, Peter; Deckers, Markus

doi:10.1016/j.bbamcr.2016.04.007

Cited by 25 publications

(25 citation statements)

References 45 publications

(68 reference statements)

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“…For assembly analyses of imported proteins, the buffer was further supplemented with 5 mM creatine phosphate and 0.1 mg/ml creatine kinase, and samples were lysed in 1% digitonin or 0.6% DDM buffer for BN-PAGE. Protein Localization Analysis-Protein localization analyses were assayed as described (27). For fluorescence microscopy analyses, yeast cells expressing Rcf3…”

Section: Methodsmentioning

confidence: 99%

“…5D, lane 8). The deletion of CYT1 leads to the loss of complex III formation leaving complex IV in its monomeric form (19,27). Under these conditions Rcf3 is still associated with the complex IV components (Fig.…”

Section: Rcf3 Is An Integral Protein Of the Mitochondrial Innermentioning

confidence: 98%

“…To address whether Rcf3 assembles into supercomplexes, we first analyzed Rcf3 interaction with complex III and IV. Therefore, we affinity-purified complex III and complex IV by IgG chromatography utilizing the ZZ-tagged structural subunits Cor1 ZZ and Cox4 ZZ (19,27). Using the mild detergent digitonin for solubilization, we were able to efficiently purify complex III/IV supercomplexes.…”

Section: Rcf3 Is An Integral Protein Of the Mitochondrial Innermentioning

confidence: 99%

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Overlapping Role of Respiratory Supercomplex Factor Rcf2 and Its N-terminal Homolog Rcf3 in Saccharomyces cerevisiae

Römpler

Müller

Juris

et al. 2016

Journal of Biological Chemistry

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Edited by Linda SpremulliThe mitochondrial electron transport chain consists of individual protein complexes arranged into large macromolecular structures, termed respiratory chain supercomplexes or respirasomes. In the yeast Saccharomyces cerevisiae, respiratory chain supercomplexes form by association of the bc 1 complex with the cytochrome c oxidase. Formation and maintenance of these assemblies are promoted by specific respiratory supercomplex factors, the Rcf proteins. For these proteins a regulatory function in bridging the electron transfer within supercomplexes has been proposed. Here we report on the maturation of Rcf2 into an N-and C-terminal peptide. We show that the previously uncharacterized Rcf3 (YBR255c-A) is a homolog of the N-terminal Rcf2 peptide, whereas Rcf1 is homologous to the C-terminal portion. Both Rcf3 and the C-terminal fragment of Rcf2 associate with monomeric cytochrome c oxidase and respiratory chain supercomplexes. A lack of Rcf2 and Rcf3 increases oxygen flux through the respiratory chain by up-regulation of the cytochrome c oxidase activity. A double gene deletion of RCF2 and RCF3 affects cellular survival under non-fermentable growth conditions, suggesting an overlapping role for both proteins in the regulation of the OXPHOS activity. Furthermore, our data suggest an association of all three Rcf proteins with the bc 1 complex in the absence of a functional cytochrome c oxidase and identify a supercomplex independent interaction network of the Rcf proteins.Eukaryotic cells cover their energy demands mainly with ATP generated by oxidative phosphorylation in mitochondria.

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Section: Methodsmentioning

confidence: 99%

Section: Rcf3 Is An Integral Protein Of the Mitochondrial Innermentioning

confidence: 98%

Section: Rcf3 Is An Integral Protein Of the Mitochondrial Innermentioning

confidence: 99%

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Overlapping Role of Respiratory Supercomplex Factor Rcf2 and Its N-terminal Homolog Rcf3 in Saccharomyces cerevisiae

Römpler

Müller

Juris

et al. 2016

Journal of Biological Chemistry

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“…Hence, it may be speculated that changes in subunit IV/Cox5 isoforms and/or binding of further protein partners or modifications such as phosphorylation might induces changes to catalysis parameters through allosteric effects of the nearby H channel by influencing its properties as a dielectric channel. An additional subunit, Cox26, has recently been found to be part of the yeast III2/IV supercomplex [Levchenco et al, 2016;Strecker et al, 2016]. A further subunit, NDUFA4, originally thought to be a subunit of complex I, has now clearly been shown to be a component of mammalian complex IV [Balsa et al, 2012] and also co-purifies with yeast III2/IV supercomplex [Vukotic et al, 2012], though its function is unknown.…”

Section: Supernumerary and Additional Subunitsmentioning

confidence: 99%

Cytochrome c Oxidase: Insight into Functions from Studies of the Yeast S. cerevisiae Homologue

Rich¹

2017

Photosynthesis and Bioenergetics

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“…Formation and stabilization of these supercomplexes is dependent on the Rcf1, Rcf2, Aac2, and Cox13 proteins (6, 9 -11). Cardiolipin (12), and the proteins Rcf3 and Cox26 are also components of supercomplexes (13)(14)(15).…”

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confidence: 99%

The Cox1 C-terminal domain is a central regulator of cytochrome c oxidase biogenesis in yeast mitochondria

García-Villegas

Camacho‐Villasana

Shingú-Vázquez

et al. 2017

Journal of Biological Chemistry

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Cytochrome oxidase (CO) is the last electron acceptor in the respiratory chain. The CO core is formed by mitochondrial DNA-encoded Cox1, Cox2, and Cox3 subunits. Cox1 synthesis is highly regulated; for example, if CO assembly is blocked, Cox1 synthesis decreases. Mss51 activates translation of mRNA and interacts with Cox1 protein in high-molecular-weight complexes (COA complexes) to form the Cox1 intermediary assembly module. Thus, Mss51 coordinates both Cox1 synthesis and assembly. We previously reported that the last 15 residues of the Cox1 C terminus regulate Cox1 synthesis by modulating an interaction of Mss51 with Cox14, another component of the COA complexes. Here, using site-directed mutagenesis of the mitochondrial gene from , we demonstrate that mutations P521A/P522A and V524E disrupt the regulatory role of the Cox1 C terminus. These mutations, as well as C terminus deletion (Cox1ΔC15), reduced binding of Mss51 and Cox14 to COA complexes. Mss51 was enriched in a translationally active form that maintains full Cox1 synthesis even if CO assembly is blocked in these mutants. Moreover, Cox1ΔC15, but not Cox1-P521A/P522A and Cox1-V524E, promoted formation of aberrant supercomplexes in CO assembly mutants lacking Cox2 or Cox4 subunits. The aberrant supercomplex formation depended on the presence of cytochrome and Cox3, supporting the idea that supercomplex assembly factors associate with Cox3 and demonstrating that supercomplexes can be formed even if CO is inactive and not fully assembled. Our results indicate that the Cox1 C-terminal end is a key regulator of CO biogenesis and that it is important for supercomplex formation/stability.

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Cox26 is a novel stoichiometric subunit of the yeast cytochrome c oxidase

Cited by 25 publications

References 45 publications

Overlapping Role of Respiratory Supercomplex Factor Rcf2 and Its N-terminal Homolog Rcf3 in Saccharomyces cerevisiae

Overlapping Role of Respiratory Supercomplex Factor Rcf2 and Its N-terminal Homolog Rcf3 in Saccharomyces cerevisiae

Cytochrome c Oxidase: Insight into Functions from Studies of the Yeast S. cerevisiae Homologue

The Cox1 C-terminal domain is a central regulator of cytochrome c oxidase biogenesis in yeast mitochondria

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