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Review
. 2004 Aug;186(16):5197-201.
doi: 10.1128/JB.186.16.5197-5201.2004.

Phosphate control of the biosynthesis of antibiotics and other secondary metabolites is mediated by the PhoR-PhoP system: an unfinished story

Juan F Martín  1
Affiliations
Review

Phosphate control of the biosynthesis of antibiotics and other secondary metabolites is mediated by the PhoR-PhoP system: an unfinished story

Juan F Martín. J Bacteriol. 2004 Aug.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Phosphate boxes and signal transduction pathway from PhoR to PhoP. (A) PhoR and PhoP consist of the following two domains: C, the carboxyl-terminal domain, and N, the amino-terminal domain. The circled P corresponds to a phosphate group. Each pho box is formed by two elements arranged in a direct repeat separated by three to seven nucleotides. Some promoters contain one pho box, whereas others contain more than one. Two pho boxes are shown in this figure. This model is based on the information available for B. subtilis (24), S. coelicolor, and S. lividans (43). (B) Nucleotide sequences of the pho boxes of E. coli and B. subtilis.
FIG. 2.
FIG. 2.
Proposed cascade mechanism involved in phosphate control of actinorhodin and undecylprodigiosin biosynthesis. The involvement of the two-component system PhoR-PhoP has been confirmed (see the text). The cascade action of AfsR mediated by AfsS on actII-ORF4 and redD pathway-specific regulators is based on the results of Umeyama and coworkers (47). The inset shows the binding of phosphorylated AfsR to the afsS promoter.
See this image and copyright information in PMC

References

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