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Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension. The resulting mutant markedly accelerates formation of the predicted triketide lactone, compared to a control in which the repositioned domain is inactive. Repositioning of the cyclase should be generally useful for redirecting polyketide synthesis to obtain polyketides of specified chain lengths., Complex polyketides are natural products, found predominantly in Streptomyces and related filamentous bacteria, that exhibit an impressive range of antibiotic, anticancer, antiparasite, and immunosuppressant activities. Despite their apparent structural diversity, [...]

We already reported the use of a long synthetic signal peptide (LSSP) to secrete the Streptomyces sp. TO1 amylase by Streptomyces lividans strain. We herein report the expression and secretion [...]

Visualizing Gene Expression in Time and Space in the Filamentous Bacterium Streptomyces coelicolor STREPTOMYCETES ARE GRAM-POSITIVE, SPORE-FORMING soil bacteria that undergo a complex cycle of morphological differentiation resembling that of [...]