Characterizing the Adenylation and Methyl-Transferase Domains of BbBSLS and BbBEAS

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Sean Johnson, Joanie M. Hevel


In nature, certain bacteria express large protein complexes referred to as Non-Ribosomal Peptide Synthetases (NRPS) which are responsible for the synthesis of natural product peptides. These synthetases often produce important biologically relevant products, such as antibiotics, siderophores, pesticides, toxins, and many others. Beauveria bassiana is a naturally occurring fungus which grows in the soil and causes white muscardine disease in many insects. Beauveria bassiana produces the NRPS termed BbBSLS, which produces the natural product bassianolide. This compound is believed to be partially responsible for the insecticidal properties of Beauveria bassiana. The BbBSLS complex possesses a unique modular arrangement, containing a methyl transferase domain inserted into the second adenylation domain. In order to understand how the structural orientation of this methyl transferase insertion relates to the overall function of the BbBSLS complex and the formation of the natural product, we have begun efforts to determine the three-dimensional structure of the methyl transferase. Once we have a greater understanding of the modular dynamics between this methyl transferase insertion and the overall synthetase activity, then we can begin to utilize this unique module as a means of tailoring other natural products for new applications, such as in the medical industry with the development of novel antibiotics.

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