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Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans
Author(s) -
Gurumoorthy Priya,
Ludwig Bernd
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13160
Subject(s) - paracoccus denitrificans , cytochrome c oxidase , biogenesis , chemistry , biology , biochemistry , enzyme , gene
Biogenesis of the mitochondrial cytochrome c oxidase ( COX ) is a complex process due to its numerous subunits encoded by two genomes, as well as the localization of redox centers deep within the membrane. Here, we have assessed the biogenesis of the homologous aa 3 ‐type oxidase of the soil bacterium Paracoccus denitrificans . First, protein partners were analyzed using various membrane solubilization strategies to show interactions between COX and CtaG, a chaperone implicated in Cu B site metallation. Using an unbiased MS approach after immunological pull‐down from untreated or cross‐linked membranes, we then extend our view towards a hypothetical ‘biogenesis complex’ by identifying two further metal‐inserting chaperones, Surf1c and Sco, together with enzymes catalyzing heme a synthesis. Our study also tentatively supports previous speculation regarding the existence of a predominantly co‐translational mechanism for cofactor insertion during COX biogenesis.