Reference: Khalimonchuk O, et al. (2010) Formation of the redox cofactor centers during Cox1 maturation in yeast cytochrome oxidase. Mol Cell Biol 30(4):1004-17

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Abstract


The biogenesis of cytochrome c oxidase initiates with synthesis and maturation of the mitochondrial-encoded Cox1 subunit prior to the addition of additional subunits. Cox1 contains redox cofactors including the low spin heme a center and the heterobimetallic heme a3:CuB center. We sought to identify the step in the maturation of Cox1 in which the redox cofactor centers were assembled. Newly synthesized Cox1 is incorporated within one early assembly intermediate containing Mss51 in Saccharomyces cerevisiae. Subsequent Cox1 maturation involves the progression to downstream assembly intermediates involving Coa1 and Shy1. We show that the two heme a cofactor sites in Cox1 form downstream of Mss51- and Coa1-containing Cox1 intermediates. These Cox1 intermediates form normally in cells defective in heme a biosynthesis or in cox1 mutant strains with heme a axial His mutations. In contrast, the Shy1-containing Cox1 assembly intermediate is perturbed in the absence of heme a. Heme a3 center formation in Cox1 appears to be chaperoned by Shy1. CuB site formation occurs near or at the Shy1-containing Cox1 assembly intermediate also. The CuB metallochaperone Cox11 transiently interacts with Shy1 by co-immunoprecipitation. The Shy1-containing Cox1 complex is markedly attenuated in cells lacking Cox11, but is partially restored with a non-functional Cox11 mutant. Thus, formation of the heterobimetallic CuB:heme a3 site likely occurs in the Shy1-containing Cox1 complex.

Reference Type
Journal Article
Authors
Khalimonchuk O, Bestwick M, Meunier B, Watts TC, Winge DR
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