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: We previously reported that S. griseus retains a phenol‐oxidizing activity and identified a laccase‐like copper‐containing extracytoplasmic oxidase EpoA (Endo et al., 2002; 2003). Based on this knowledge, the scoC mutant of S. griseus was assessed for extracellular phenol‐oxidizing activity by using N,N′‐dimethyl‐p‐phenylenediamine sulfate (DMP) as a substrate (Experimental procedures). The DMP‐oxidizing activity in the crude extract of the scoC mutant cells was lower than that in the wild‐type cells (Fig. 6). A marked DMP‐oxidizing activity was restored in this mutant by supplying 10 µM CuSO4 to the culture medium.
Affiliation: Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Japan.