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A High-throughput Automated Platform for the Development of Manufacturing Cell Lines for Protein Therapeutics
Published on: September 22, 2011
Cloning, purification and characterization of a functional anthracycline glycosyltransferase
Giorgos Sianidis1, Sven-Eric Wohlert, Charalambos Pozidis
1Institute of Molecular Biology and Biotechnology, FORTH and Department of Biology, University of Crete, P.O. Box 1527, Iraklio-Crete 71110, Greece.
Abstract:
We have cloned the gene that encodes a novel glucosyl transferase (AraGT) involved in rhamnosylation of the polyketide antibiotic Aranciamycin in Streptomyces echinatus. AraGT comprises two domains characteristic of bacterial glycosyltranferases. AraGT was synthesized in E. coli as a decahistidinyl-tagged polypeptide. Purified AraGT is dimeric, displays a T(mapp) of 30 degrees C and can glycosylate the aglycone of an Aranciamycin derivative as shown by liquid chromatography and mass spectrometry. The availability of functional AraGT will allow the generation Aranciamycin-based combinatorial libraries.
