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Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces.

Fujimoto M, Yamada A, Kurosawa J, Kawata A, Beppu T, Takano H, Ueda K - Microb Biotechnol (2011)

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.

View Article: PubMed Central - PubMed

Affiliation: Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Japan.

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DMP‐oxidizing activity of S. griseus. The wild‐type strain and scoC mutant of S. griseus grown for 5 days in Bennett's/maltose solid medium (without/with 10 µM CuSO4) were studied for DMP‐oxidizing activity by measuring the increment of absorbance at 550 nm (Endo et al., 2003).
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f6: DMP‐oxidizing activity of S. griseus. The wild‐type strain and scoC mutant of S. griseus grown for 5 days in Bennett's/maltose solid medium (without/with 10 µM CuSO4) were studied for DMP‐oxidizing activity by measuring the increment of absorbance at 550 nm (Endo et al., 2003).

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.


Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces.

Fujimoto M, Yamada A, Kurosawa J, Kawata A, Beppu T, Takano H, Ueda K - Microb Biotechnol (2011)

DMP‐oxidizing activity of S. griseus. The wild‐type strain and scoC mutant of S. griseus grown for 5 days in Bennett's/maltose solid medium (without/with 10 µM CuSO4) were studied for DMP‐oxidizing activity by measuring the increment of absorbance at 550 nm (Endo et al., 2003).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815325&req=5

f6: DMP‐oxidizing activity of S. griseus. The wild‐type strain and scoC mutant of S. griseus grown for 5 days in Bennett's/maltose solid medium (without/with 10 µM CuSO4) were studied for DMP‐oxidizing activity by measuring the increment of absorbance at 550 nm (Endo et al., 2003).
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.

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.

View Article: PubMed Central - PubMed

Affiliation: Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Japan.

Show MeSH
Related in: MedlinePlus