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J. Bacteriol., Feb 1997, 705-713, Vol 179, No. 3
Copyright © 1997, American Society for Microbiology

Pristinamycin I biosynthesis in Streptomyces pristinaespiralis: molecular characterization of the first two structural peptide synthetase genes

V de Crecy-Lagard, V Blanc, P Gil, L Naudin, S Lorenzon, A Famechon, N Bamas- Jacques, J Crouzet and D Thibaut
Division Recherche Pharmaceutique, Centre de Recherche de Vitry- Alfortville, Rhone Poulenc Rorer S.A., Vitry-sur-Seine, France. vcrecy@pasteur.fr

Two genes involved in the biosynthesis of the depsipeptide antibiotics pristinamycins I (PI) produced by Streptomyces pristinaespiralis were cloned and sequenced. The 1.7-kb snbA gene encodes a 3-hydroxypicolinic acid:AMP ligase, and the 7.7-kb snbC gene encodes PI synthetase 2, responsible for incorporating L-threonine and L-aminobutyric acid in the PI macrocycle. snbA and snbC, which encode the two first structural enzymes of PI synthesis, are not contiguous. Both genes are located in PI-specific transcriptional units, as disruption of one gene or the other led to PI-deficient strains producing normal levels of the polyunsaturated macrolactone antibiotic pristinamycin II, also produced by S. pristinaespiralis. Analysis of the deduced amino acid sequences showed that the SnbA protein is a member of the adenylate-forming enzyme superfamily and that the SnbC protein contains two amino acid- incorporating modules and a C-terminal epimerization domain. A model for the initiation of PI synthesis analogous to the established model of initiation of fatty acid synthesis is proposed.


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