Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces.
Bottom Line: The scoC mutant of S. griseus was also defective in the extracellular activity oxidizing N,N'-dimethyl-p-phenylenediamine sulfate.Addition of 10 µM CuSO(4) repressed the activity of the conserved promoter preceding scoA and caused phenylalanine auxotrophy in some Streptomyces spp. probably because of the repression of pheA; pheA encodes prephenate dehydratase, which is located at the 3' terminus of the putative operon structure.Overall, the evidence indicates that Sco is crucial for the utilization of copper under a low-copper condition and for the activation of the multiple Cu(2+) -containing oxidases that play divergent roles in the complex physiology of Streptomyces.
Affiliation: Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Japan.Show MeSH
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Mentions: Because Sco1/SenC proteins are involved in the incorporation of copper into cox, its activity was measured using N,N,N′,N′‐tetramethyl‐p‐phenylenediamine (TMPD; see Experimental procedures) with respect to the cells grown in the aforementioned conditions. As shown in Fig. 4A (upper), the wild type of S. coelicolor exhibited high cox activities during early growth phases in Bennett's/glucose medium. In contrast, the scoC mutant exhibited remarkably low activities. The activity in the scoC mutant, however, was restored by the addition of 10 µM CuSO4, to a level higher than that of the wild type, and this restoration by CuSO4 was abolished by the addition of 400 µM BCDA. A similar cox activity profile was obtained with respect to scoC mutant of S. griseus (Fig. 4A, lower).
Affiliation: Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Japan.