Role of Copper Ions in the Regulation of<scp>L</scp>-Glutamate Biosynthesis

Sugiyama, Yoshio; Kitano, Kazuaki; Kanzaki, Toshihiko

doi:10.1080/00021369.1973.10860919

Cited by 4 publications

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“…At the same time, the cytochrome a peak at 602 nm was reduced and slightly blue-shifted, and the cytochrome c peak at 552 nm was reduced. These changes are in agreement with previous data (28) and show that copper deprivation has a severe influence on the composition of the respiratory chain.…”

Section: Biogenesis Of Actinobacterial Cytochrome C Oxidasesupporting

confidence: 93%

“…As a starting point in our search for proteins involved in copper insertion into cytochrome aa 3 oxidase, we determined the copper-deprivation stimulon of C. glutamicum and analyzed genes with increased expression. Copper deprivation is known to influence the content of cytochrome aa 3 oxidase in various bacteria (27,28). Using this approach, two candidate proteins were identified and characterized, CtiP (Cg2699) and CopC (Cg1884).…”

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The copper-deprivation stimulon of Corynebacterium glutamicum comprises proteins for biogenesis of the actinobacterial cytochrome bc1–aa3 supercomplex

Morosov

Davoudi

Baumgart

et al. 2018

Journal of Biological Chemistry

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Aerobic respiration in involves a cytochrome - supercomplex with a diheme cytochrome , which is the only-type cytochrome in this species. This organization is considered as typical for aerobic Actinobacteria. Whereas the biogenesis of heme-copper type oxidases like cytochrome has been studied extensively in α-proteobacteria, yeast, and mammals, nothing is known about this process in Actinobacteria. Here, we searched for assembly proteins of the supercomplex by identifying the copper-deprivation stimulon, which might include proteins that insert copper into cytochrome Using gene expression profiling, we found two copper starvation-induced proteins for supercomplex formation. The Cg2699 protein, named CtiP, contained 16 predicted transmembrane helices, and its sequence was similar to that of the copper importer CopD of in the N-terminal half and to the cytochrome oxidase maturation protein CtaG of in its C-terminal half. CtiP deletion caused a growth defect similar to that produced by deletion of subunit I of cytochrome , increased copper tolerance, triggered expression of the copper-deprivation stimulon under copper sufficiency, and prevented co-purification of the supercomplex subunits. The secreted Cg1884 protein, named CopC, had a C-terminal transmembrane helix and contained a Cu(II)-binding motif. Its absence caused a conditional growth defect, increased copper tolerance, and also prevented co-purification of the supercomplex subunits. CtiP and CopC are conserved among aerobic Actinobacteria, and we propose a model of their functions in cytochrome biogenesis. Furthermore, we found that the copper-deprivation response involves additional regulators besides the ECF sigma factor SigC.

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Section: Biogenesis Of Actinobacterial Cytochrome C Oxidasesupporting

confidence: 93%

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confidence: 99%