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Type II thioesterase from Streptomyces coelicolor A3(2)

Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland¹
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK²
Department of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK³

Author for correspondence: Katarzyna Kuczek. Tel: +48 71 3732274. Fax: +48 71 373 2587. e-mail: kuczek{at}immuno.iitd.pan.wroc.pl

Type I polyketide synthases (PKSs) are complexes of large, multimodular enzymes that catalyse biosynthesis of polyketide compounds via repetitive reaction sequences, during which each step is catalysed by a separate enzymic domain. Many type I PKSs, and also non-ribosomal peptide synthetase clusters, contain additional thioesterase genes located adjacent to PKS genes. These are discrete proteins called type II thioesterases (TE IIs) to distinguish them from chain-terminating thioesterase (TE I) domains that are usually fused to the terminal PKS module. A gene of a new TE II, scoT, associated with the cluster of putative type I PKS genes from Streptomyces coelicolor A3(2), was found. The deduced amino acid sequence of the gene product shows extensive similarity to other authentic thioesterase enzymes, including conservation of characteristic motifs and residues involved in catalysis. When expressed in the heterologous host Streptomyces fradiae, scoT successfully complemented the resident TE II gene (tylO), and, by restoring a significant level of macrolide production, proved to be catalytically equivalent to the TylO protein. S₁ nuclease mapping of scoT revealed a single potential transcription start point with expression being switched on for a short period of time during a transition phase of growth.

Keywords: thioesterase type II, Streptomyces fradiae, disruption mutant complementation, S₁ nuclease mapping

Abbreviations: PKS, polyketide synthase; TE, thioesterase

The GenBank accession number for the sequence reported in this paper is AF109727.

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