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Journal of Bacteriology, September 2006, p. 6269-6276, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00202-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Regulation of ppk Expression and In Vivo Function of Ppk in Streptomyces lividans TK24

Sofiane Ghorbel,1 Aleksey Smirnov,2 Hichem Chouayekh,3 Brice Sperandio,4 Catherine Esnault,6 Jan Kormanec,5 and Marie-Joelle Virolle6*

University of Kansas Medical Center, Department of Microbiology, Immunology and Molecular Genetics, 3901 Rainbow Boulevard, Kansas City, Kansas 66160,1 G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russia,2 Centre de Biotechnologie de Sfax, Route de Soukra Km 4,5, 3038 Sfax, Tunisia,3 Institut National de la Recherche Agronomique, Laboratoire de Génétique Microbienne, 78352 Jouy-en-Josas, France,4 Institute of Molecular Biology, Dubravska cesta 21, 845 51 Bratislava, Slovak Republic,5 Institut de Génétique et Microbiologie, Université Paris XI, 91405 Orsay, France6

Received 7 February 2006/ Accepted 10 April 2006

The ppk gene of Streptomyces lividans encodes an enzyme catalyzing, in vitro, the reversible polymerization of the {gamma} phosphate of ATP into polyphosphate and was previously shown to play a negative role in the control of antibiotic biosynthesis (H. Chouayekh and M. J. Virolle, Mol. Microbiol. 43:919-930, 2002). In the present work, some regulatory features of the expression of ppk were established and the polyphosphate content of S. lividans TK24 and the ppk mutant was determined. In Pi sufficiency, the expression of ppk was shown to be low but detectable. DNA gel shift experiments suggested that ppk expression might be controlled by a repressor using ATP as a corepressor. Under these conditions, short acid-soluble polyphosphates accumulated upon entry into the stationary phase in the wild-type strain but not in the ppk mutant strain. The expression of ppk under Pi-limiting conditions was shown to be much higher than that under Pi-sufficient conditions and was under positive control of the two-component system PhoR/PhoP. Under these conditions, the polyphosphate content of the cell was low and polyphosphates were reproducibly found to be longer and more abundant in the ppk mutant strain than in the wild-type strain, suggesting that Ppk might act as a nucleoside diphosphate kinase. In light of our results, a novel view of the role of this enzyme in the regulation of antibiotic biosynthesis in S. lividans TK24 is proposed.

* Corresponding author. Mailing address: Laboratoire de Métabolisme Energétique des Streptomyces, Institut de Génétique et Microbiologie, UMR CNRS 8621, Bâtiment 400 de l'Université Paris Sud, 91405 Orsay, France. Phone: 33 (0) 1 69 15 46 42. Fax: 33 (0) 1 69 15 45 44. E-mail: marie-joelle.virolle{at}igmors.u-psud.fr.

Journal of Bacteriology, September 2006, p. 6269-6276, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00202-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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