Coi1 is a novel assembly factor of the yeast complex III–complex IV supercomplex

Singhal, Ravi Kumar; Kruse, Christine; Heidler, Juliana; Strecker, Valentina; Zwicker, Klaus; Düsterwald, Lea; Westermann, Benedikt; Herrmann, Johannes M.; Wittig, Ilka; Rapaport, Doron

doi:10.1091/mbc.e17-02-0093

Cited by 15 publications

(19 citation statements)

References 37 publications

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“…It is interesting to mention that there are diverse specific regulatory proteins for the supramolecular organization of individual complexes that include CIV [ 73 ], respiratory SC factors 1 and 2 (Rcf1 and 2) [ 74 ], protein Cox interacting (Coi) [ 75 ], and COX7a2L [ 76 ]. These proteins downregulation can impair the formation of SC; for instance, some studies show that diverse pathologies decrease CIV subunit levels affecting stoichiometry and assembly of SC [ 77 , 78 ].…”

Section: Resultsmentioning

confidence: 99%

Streptozotocin-Induced Adaptive Modification of Mitochondrial Supercomplexes in Liver of Wistar Rats and the Protective Effect ofMoringa oleiferaLam

Sánchez-Muñoz

Valdez-Solana

Campos-Almazán

et al. 2018

Biochemistry Research International

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The increasing prevalence of diabetes continues to be a major health issue worldwide. Alteration of mitochondrial electron transport chain is a recognized hallmark of the diabetic-associated decline in liver bioenergetics; however, the molecular events involved are only poorly understood. Moringa oleifera is used for the treatment of diabetes. However, its role on mitochondrial functionality is not yet established. This study was aimed to evaluate the effect of M. oleifera extract on supercomplex formation, ATPase activity, ROS production, GSH levels, lipid peroxidation, and protein carbonylation. The levels of lipid peroxidation and protein carbonylation were increased in diabetic group. However, the levels were decreased in Moringa-treated diabetic rats. Analysis of in-gel activity showed an increase in all complex activities in the diabetic group, but spectrophotometric determinations of complex II and IV activities were unaffected in this treatment. However, we found an oxygen consumption abolition through complex I-III-IV pathway in the diabetic group treated with Moringa. While respiration with succinate feeding into complex II-III-IV was increased in the diabetic group. These findings suggest that hyperglycemia modifies oxygen consumption, supercomplexes formation, and increases ROS levels in mitochondria from the liver of STZ-diabetic rats, whereas M. oleifera may have a protective role against some alterations.

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Section: Resultsmentioning

confidence: 99%

Streptozotocin-Induced Adaptive Modification of Mitochondrial Supercomplexes in Liver of Wistar Rats and the Protective Effect ofMoringa oleiferaLam

Sánchez-Muñoz

Valdez-Solana

Campos-Almazán

et al. 2018

Biochemistry Research International

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“…The function of respiratory supercomplexes is debated with proposals ranging from substrate channeling over a decrease in ROS to avoiding aggregation of proteins in the crowded inner mitochondrial membrane (IMM) (Genova and Lenaz, 2014;Milenkovic et al, 2017;Fedor et al, 2018;Lobo-Jarne and Ugalde, 2018). Several proteins were found to associate with the respiratory supercomplexes without being a subunit of the individual complexes, namely Coi1, Aac2, Rcf1, and Rcf2 (Claypool et al, 2008;Dienhart and Stuart, 2008;Chen et al, 2012;Strogolova et al, 2012;Vukotic et al, 2012;Singhal et al, 2017). Recent cryo-EM structures of the yeast supercomplexes could not resolve these proteins interacting with the complexes (Letts et al, 2016;Hartley et al, 2019;Rathore et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Rcf1 Modulates Cytochrome c Oxidase Activity Especially Under Energy-Demanding Conditions

et al. 2020

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The mitochondrial respiratory chain is assembled into supercomplexes. Previously, two respiratory supercomplex-associated proteins, Rcf1 and Rcf2, were identified in Saccharomyces cerevisiae, which were initially suggested to mediate supercomplex formation. Recent evidence suggests that these factors instead are involved in cytochrome c oxidase biogenesis. We demonstrate here that Rcf1 mediates proper function of cytochrome c oxidase, while binding of Rcf2 results in a decrease of cytochrome c oxidase activity. Chemical crosslink experiments demonstrate that the conserved Hig-domain as well as the fungi specific C-terminus of Rcf1 are involved in molecular interactions with the cytochrome c oxidase subunit Cox3. We propose that Rcf1 modulates cytochrome c oxidase activity by direct binding to the oxidase to trigger changes in subunit Cox1, which harbors the catalytic site. Additionally, Rcf1 interaction with cytochrome c oxidase in the supercomplexes increases under respiratory conditions. These observations indicate that Rcf1 could enable the tuning of the respiratory chain depending on metabolic needs or repair damages at the catalytic site.

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“…Twelve of them have catalytic activity, two are part of mitochondrial transmembrane transport (Tom40 and Mic60) and one of unknown function but a major constituent of the outer mitochondrial membrane (OM45). According to Singhal et al, Tom40, Mic60, and OM45, as a part of yeast's respiratory supercomplexes interact with Coi1, a novel assembly factor of the yeast complex III to complex IV supercomplex. In this work, the expression of Mic60 increased, while that of OM45 and Tom40 decreased, probably as a consequence of reformation assembly process of the single complexes.…”

Section: Resultsmentioning

confidence: 99%

“…In this work, the expression of Mic60 increased, while that of OM45 and Tom40 decreased, probably as a consequence of reformation assembly process of the single complexes. The composition of the various supercomplexes might change depending on cell types and their physiological needs . In detailed mitochondrial proteomic studies of Morgenstern et al approved identification and functional characterization of submitochondrial proteins under different growth conditions were presented.…”

Section: Resultsmentioning

confidence: 99%

Combining proteomics and lipid analysis to unravel Confidor stress response in Saccharomyces cerevisiae

Justinić

Katić

Uršičić

et al. 2019

Environmental Toxicology

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The yeast Saccharomyces cerevisiae is a useful model for studying the influence of different stress factors on eukaryotic cells. In this work we used the pesticide imidacloprid, in the Confidor formulation, as the stress factor and analyzed its influence on the metabolic activity, proteome and lipid content and composition of Saccharomyces cerevisiae yeast. During the cultivation of yeast, the lowest recommended application dose of Confidor (0.025%, v/v) was added to the growth media and its influence on the mitochondria, cytosol with microsomes, and the whole yeast cells was monitored. The results show that under the stress provoked by the toxic effects of Confidor, yeast cells density significantly decreased and the percentage of metabolically disturbed cells significantly increased comparing with untreated control.Also, there was a downregulation of majority of glycolytic, gluconeogenesis, and TCA cycle enzymes (Fba1, Adh1, Hxk2, Tal1, Tdh1,Tdh3, Eno1) thus providing enough acetyl-CoA for the lipid restructuring and accumulation mechanism since we have found the changes in the cell and mitochondrial lipid content and FA composition.This data suggest that lipids could be the molecules that orchestrate the answer of the cells in the stress response to the Confidor treatment.

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Coi1 is a novel assembly factor of the yeast complex III–complex IV supercomplex

Cited by 15 publications

References 37 publications

Streptozotocin-Induced Adaptive Modification of Mitochondrial Supercomplexes in Liver of Wistar Rats and the Protective Effect ofMoringa oleiferaLam

Streptozotocin-Induced Adaptive Modification of Mitochondrial Supercomplexes in Liver of Wistar Rats and the Protective Effect ofMoringa oleiferaLam

Rcf1 Modulates Cytochrome c Oxidase Activity Especially Under Energy-Demanding Conditions

Combining proteomics and lipid analysis to unravel Confidor stress response in Saccharomyces cerevisiae

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