1887

Abstract

The Gram-positive bacterium contains two respiratory oxidases of the haem-copper superfamily: cytochrome , which is a quinol oxidase, and cytochrome , which is a cytochrome oxidase. Cytochrome oxidase uniquely contains a di-copper centre, Cu. CtaG is a membrane protein encoded by the same gene cluster as that which encodes the subunits of cytochrome oxidase. The role of CtaG and orthologous proteins present in many other Gram-positive bacteria has remained unexplored. The sequence of CtaG is unrelated to that of CtaG/Cox11p of proteobacteria and eukaryotic cells. This study shows that CtaG is essential for the formation of active cytochrome but is not required for assembly of the core subunits I and II with haem in the membrane and it has no role in the synthesis of active cytochrome . YpmQ, a homologue to Sco1p of eukaryotic cells, is also a membrane-bound cytochrome oxidase-specific assembly factor. Properties of CtaG- and YpmQ-deficient mutants were compared. Cells lacking YpmQ showed a low cytochrome oxidase activity and this defect was suppressed by the supplementation of the growth medium with copper ions. It has previously been proposed that YpmQ/Sco1p is involved in synthesis of the Cu centre. The results of this study are consistent with this proposal but the exact role of YpmQ in assembly of cytochrome oxidase remains to be elucidated.

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2004-02-01
2019-10-15
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