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PMID:22342701

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Citation

Vukotic, M, Oeljeklaus, S, Wiese, S, Vögtle, FN, Meisinger, C, Meyer, HE, Zieseniss, A, Katschinski, DM, Jans, DC, Jakobs, S, Warscheid, B, Rehling, P and Deckers, M (2012) Rcf1 mediates cytochrome oxidase assembly and respirasome formation, revealing heterogeneity of the enzyme complex. Cell Metab. 15:336-47

Abstract

The terminal enzyme of the mitochondrial respiratory chain, cytochrome oxidase, transfers electrons to molecular oxygen, generating water. Within the inner mitochondrial membrane, cytochrome oxidase assembles into supercomplexes, together with other respiratory chain complexes, forming so-called respirasomes. Little is known about how these higher oligomeric structures are attained. Here we report on Rcf1 and Rcf2 as cytochrome oxidase subunits in S. cerevisiae. While Rcf2 is specific to yeast, Rcf1 is a conserved subunit with two human orthologs, RCF1a and RCF1b. Rcf1 is required for growth in hypoxia and complex assembly of subunits Cox13 and Rcf2, as well as for the oligomerization of a subclass of cytochrome oxidase complexes into respirasomes. Our analyses reveal that the cytochrome oxidase of mitochondria displays intrinsic heterogeneity with regard to its subunit composition and that distinct forms of respirasomes can be formed by complex variants.

Links

PubMed Online version:10.1016/j.cmet.2012.01.016

Keywords

Electron Transport Complex IV/genetics; Electron Transport Complex IV/metabolism; Immunoprecipitation; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:COX13

involved_in

GO:0097250: mitochondrial respirasome assembly

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:RCF2

located_in

GO:0031305: integral component of mitochondrial inner membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:RCF2

located_in

GO:0005746: mitochondrial respirasome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:RCF1

located_in

GO:0031305: integral component of mitochondrial inner membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:RCF1

located_in

GO:0005746: mitochondrial respirasome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:COX26

located_in

GO:0005743: mitochondrial inner membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:COX4

GO:0033617: mitochondrial respiratory chain complex IV assembly

ECO:0000315:

P

Figure 2 (B). The lack of band in lane 14 and 16 compared to the WT bands at the specific high molecular weight of 230 and 440 kDa indicates the lack of complex IV in mutant cox4.

complete
CACAO 4883

YEAST:COX4

involved_in

GO:0033617: mitochondrial respiratory chain complex IV assembly

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:RCF1

GO:0097250: mitochondrial respiratory chain supercomplex assembly

ECO:0000315:

P

Figure 4 (B) and 4(D). Dramatic lost of III2 and IV2 complex can be seen in the lanes of the rcf1 mutant when compared to the wildtype lanes.

complete
CACAO 4893

YEAST:RCF1

part_of

GO:0005746: mitochondrial respirasome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

YEAST:RCF1

involved_in

GO:0097250: mitochondrial respirasome assembly

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:RCF1

part_of

GO:0031305: integral component of mitochondrial inner membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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