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KMID : 0545120030130050823
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Journal of Microbiology and Biotechnology
2003 Volume.13 No. 5 p.823 ~ p.827
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Site-Directed Mutagenesis on Putative Macrolactone Ring Size Determinant in the Hybrid Pikromycin-Tylosin Polyketide Synthase
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JUNG, WON-SEOK
KIM, EUNG-SOO/KANG, HAN-YOUNG/CHOI, CHA-YONG/SHERMAN, DAVID H./YOON, YEO JOON
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Abstract
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Streptomyces venezuelae ATCC 15439 is notable in its ability to produce two distinct groups of macrolactones. It has been reported that the generation of two macrolactone structures results from alternative expression of pikromycin (Pik) polyketide synthase (PKS). It was previously reported that the hybrid pikromycin-tylosin PKS can also produce two different macrolactones but its mechanistic basis remains unclear. In order to address this question, a series of site-directed mutagenesis of tentative alternative ribosome binding site and translation start codons in rylGV were performed. The results suggest that macrolactone ring size is not determined by the alternative expression of Ty/GV but through other mechanism(s) involving direct interaction between the PikAⅢ and TE domain or skipping of the final chain elongation step. This provides new insight into the mechanism of macrolactone ring size determination in hybrid PKS as well as an opportunity to develop novel termination activities for combinatorial biosynthesis.
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