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YtkA (CtaK) and YozB (CtaM) function in the biogenesis of cytochrome c oxidase in Bacillus subtilis
Author(s) -
Wachenfeldt Claes,
Hallgren Joel,
Hederstedt Lars
Publication year - 2021
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14701
Subject(s) - biology , cytochrome c oxidase , biochemistry , cytochrome , bacillus subtilis , heme a , heme , electron transport complex iv , oxidase test , cytochrome b , cytochrome p450 reductase , cytochrome c , coenzyme q – cytochrome c reductase , cytochrome c1 , periplasmic space , respiratory chain , mitochondrion , bacteria , enzyme , gene , escherichia coli , genetics , mitochondrial dna
Cytochrome c oxidase in the respiratory chain of bacteria and mitochondria couples the reduction of molecular oxygen to form water with the generation of a transmembrane proton gradient. Bacillus subtilis has two heme A‐containing heme–copper oxidases: the menaquinol oxidase cytochrome aa 3 and the cytochrome c oxidase cytochrome caa 3 . By screening three collections of mutants for defective cytochrome c oxidase, we found the genes for two, new membrane‐bound assembly factors in B . subtilis : ytkA and yozB (renamed ctaK and ctaM , respectively). CtaK is a lipoprotein without sequence similarity to any protein of known function. We show that CtaK functions together with Sco1 (YpmQ) in a pathway, leading to the assembly of the Cu A center in cytochrome caa 3 and seems to be a functional analogue to proteins of the periplasmic Cu A chaperone family (PCu A C). CtaM is required for the activity of both cytochrome caa 3 and cytochrome aa 3 and dispensable for the insertion of heme A into these oxidases. The orthologous Bacillus anthracis protein and the distantly related Staphylococcus aureus CtaM complemented CtaM deficiency in B. subtilis, establishing a common function of CtaM in these bacteria. As the overall result of our work, 12 different proteins are known to function in the biosynthesis of cytochrome c oxidase in B. subtilis .