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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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Cox activity of the sco mutants. A. Transition of cox activity in the wild‐type strain and the scoC mutant of S. coelicolor A3(2) (upper) and S. griseus (lower). TMPD‐oxidizing activity was measured with respect to the cells grown for 24, 48 and 72 h in Bennett's/glucose (S. coelicolor) or YMP/glucose (S. griseus) liquid medium supplied with neither CuSO4 nor BCDA (open circle), 10 µM CuSO4 (open triangle), or 10 µM CuSO4 and 400 µM (S. coelicolor) or 200 µM (S. griseus) BCDA (open square). Data are means of duplicated measurements. B. Cox activity of the other sco mutants of S. coelicolor A3(2). Each mutant was grown in Bennett's/glucose and maltose liquid medium supplied without and with 400 µM BCDA for 24 h, and studied for TMPD‐oxidizing activity. Data for the wild type and scoC mutant are also shown.
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f4: Cox activity of the sco mutants. A. Transition of cox activity in the wild‐type strain and the scoC mutant of S. coelicolor A3(2) (upper) and S. griseus (lower). TMPD‐oxidizing activity was measured with respect to the cells grown for 24, 48 and 72 h in Bennett's/glucose (S. coelicolor) or YMP/glucose (S. griseus) liquid medium supplied with neither CuSO4 nor BCDA (open circle), 10 µM CuSO4 (open triangle), or 10 µM CuSO4 and 400 µM (S. coelicolor) or 200 µM (S. griseus) BCDA (open square). Data are means of duplicated measurements. B. Cox activity of the other sco mutants of S. coelicolor A3(2). Each mutant was grown in Bennett's/glucose and maltose liquid medium supplied without and with 400 µM BCDA for 24 h, and studied for TMPD‐oxidizing activity. Data for the wild type and scoC mutant are also shown.

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).


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)

Cox activity of the sco mutants. A. Transition of cox activity in the wild‐type strain and the scoC mutant of S. coelicolor A3(2) (upper) and S. griseus (lower). TMPD‐oxidizing activity was measured with respect to the cells grown for 24, 48 and 72 h in Bennett's/glucose (S. coelicolor) or YMP/glucose (S. griseus) liquid medium supplied with neither CuSO4 nor BCDA (open circle), 10 µM CuSO4 (open triangle), or 10 µM CuSO4 and 400 µM (S. coelicolor) or 200 µM (S. griseus) BCDA (open square). Data are means of duplicated measurements. B. Cox activity of the other sco mutants of S. coelicolor A3(2). Each mutant was grown in Bennett's/glucose and maltose liquid medium supplied without and with 400 µM BCDA for 24 h, and studied for TMPD‐oxidizing activity. Data for the wild type and scoC mutant are also shown.
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Related In: Results  -  Collection

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f4: Cox activity of the sco mutants. A. Transition of cox activity in the wild‐type strain and the scoC mutant of S. coelicolor A3(2) (upper) and S. griseus (lower). TMPD‐oxidizing activity was measured with respect to the cells grown for 24, 48 and 72 h in Bennett's/glucose (S. coelicolor) or YMP/glucose (S. griseus) liquid medium supplied with neither CuSO4 nor BCDA (open circle), 10 µM CuSO4 (open triangle), or 10 µM CuSO4 and 400 µM (S. coelicolor) or 200 µM (S. griseus) BCDA (open square). Data are means of duplicated measurements. B. Cox activity of the other sco mutants of S. coelicolor A3(2). Each mutant was grown in Bennett's/glucose and maltose liquid medium supplied without and with 400 µM BCDA for 24 h, and studied for TMPD‐oxidizing activity. Data for the wild type and scoC mutant are also shown.
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).

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