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Microbiology 155 (2009), 1800-1811; DOI  10.1099/mic.0.026799-0
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Microbiology 155 (2009), 1800-1811; DOI  10.1099/mic.0.026799-0
© 2009 Society for General Microbiology

Phosphate and carbon source regulation of two PhoP-dependent glycerophosphodiester phosphodiesterase genes of Streptomyces coelicolor

Fernando Santos-Beneit1, Antonio Rodríguez-García1,2, Alexander K. Apel1 and Juan F. Martín1,2

1 Instituto de Biotecnología de León, INBIOTEC, Parque Científico de León, Av. Real 1, 24006 León, Spain
2 Área de Microbiología, Fac. CC. Biológicas y Ambientales, Universidad de León, Campus de Vegazana s/n, 24071 León, Spain

Glycerophosphodiesters are formed by deacylation of phospholipids. Streptomyces coelicolor and other soil-dwelling actinomycetes utilize glycerophosphodiesters as phosphate and carbon sources by the action of glycerophosphodiester phosphodiesterases (GDPDs). Seven genes encoding putative GDPDs occur in the S. coelicolor genome. Two of these genes, glpQ1 and glpQ2, encoding extracellular GDPDs, showed a PhoP-dependent upregulated profile in response to phosphate shiftdown. Expression studies using the luxAB genes as reporter confirmed the PhoP dependence of both glpQ1 and glpQ2. Footprinting analyses with pure GST-PhoP of the glpQ1 promoter revealed four protected direct repeat units (DRu). PhoP binding affinity to the glpQ2 promoter was lower and revealed a protected region containing five DRu. As expected for pho regulon genes, inorganic phosphate, and also glycerol 3-phosphate, inhibited the expression from both glpQ1 and glpQ2. The expression of glpQ1 was also repressed by serine and inositol but expression of glpQ2 was not. In contrast, glucose, fructose and glycerol increased expression of glpQ2 but not that of glpQ1. In summary, our results suggest an interaction of phosphate control mediated by PhoP and carbon source regulation of the glpQ1 and glpQ2 genes involving complex operator structures.

Correspondence
Juan F. Martín
jf.martin{at}unileon.es

Abbreviations: CCR, carbon catabolite regulation; DRu, direct repeat unit(s); EMSA, electrophoretic mobility shift assay; G3P, sn-glycerol 3-phosphate; GDPD, glycerophosphodiester phosphodiesterase; GST, glutathione S-transferase; TSP, transcription start point






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