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TitleRcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 17, Page 9329-9337, Year 2020
Publish dateApr 28, 2020
AuthorsAndrew M Hartley / Brigitte Meunier / Nikos Pinotsis / Amandine Maréchal /
PubMed AbstractThe organization of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed; however, their assembly process, or the role of differential expression isoforms, ...The organization of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed; however, their assembly process, or the role of differential expression isoforms, remain to be determined. In , cytochrome oxidase (CIV) forms SCs of varying stoichiometry with cytochrome (CIII). Recent studies have revealed, in normoxic growth conditions, an interface made exclusively by Cox5A, the only yeast respiratory protein that exists as one of two isoforms depending on oxygen levels. Here we present the cryo-EM structures of the III-IV and III-IV SCs containing the hypoxic isoform Cox5B solved at 3.4 and 2.8 Å, respectively. We show that the change of isoform does not affect SC formation or activity, and that SC stoichiometry is dictated by the level of CIII/CIV biosynthesis. Comparison of the CIV- and CIV-containing SC structures highlighted few differences, found mainly in the region of Cox5. Additional density was revealed in all SCs, independent of the CIV isoform, in a pocket formed by Cox1, Cox3, Cox12, and Cox13, away from the CIII-CIV interface. In the CIV-containing hypoxic SCs, this could be confidently assigned to the hypoxia-induced gene 1 (Hig1) type 2 protein Rcf2. With conserved residues in mammalian Hig1 proteins and Cox3/Cox12/Cox13 orthologs, we propose that Hig1 type 2 proteins are stoichiometric subunits of CIV, at least when within a III-IV SC.
External linksProc Natl Acad Sci U S A / PubMed:32291341 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.41 Å
Structure data

EMDB-10317:
Complex III of the III2-IV(5B)1 respiratory supercomplex from S. cerevisiae after focused refinement
Method: EM (single particle) / Resolution: 3.29 Å

10318

6t15

EMDB-10318: Complex IV of the III2-IV5B1 respiratory supercomplex from S. cerevisiae after focused refinement
PDB-6t15: The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae
Method: EM (single particle) / Resolution: 3.41 Å

EMDB-10334:
Complex IV in the III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae (CIV(5B)-b)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-10335:
CIV1 of the III2-IV5B2 respiratory supercomplex from S. cerevisiae after focused refinement
Method: EM (single particle) / Resolution: 2.8 Å

10340

6t0b

EMDB-10340, PDB-6t0b:
The III2-IV(5B)2 respiratory supercomplex from S. cerevisiae
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-10375:
Complex IV in the III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae (CIV(5A)-a)
Method: EM (single particle) / Resolution: 3.09 Å

EMDB-10376:
Complex IV in the III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae (CIV(5A)-b)
Method: EM (single particle) / Resolution: 3.24 Å

Chemicals

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-PEF:
DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-PCF:
1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE / Dipalmitoylphosphatidylcholine

ChemComp-HEC:
HEME C / Heme C

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-HEA:
HEME-A / Heme A

ChemComp-CA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-CUA:
DINUCLEAR COPPER ION

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsOXIDOREDUCTASE / CYTOCHROME C OXIDASE CYTOCHROME BC1 MITOCHONDRIA RESPIRATORY CHAIN SUPERCOMPLEX / ELECTRON TRANSPORT / OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX

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