BIOL 127 |
| Carrier proteins are central players in many primary and secondary metabolism pathways including the biosynthesis of fatty acids, polyketides, and non-ribosomal peptides. The carrier protein acts as a scaffold for the growing natural products tethering them via attachment to the thiol terminus of a phosphopantetheine arm. This appendage is derived from co-enzyme A and posttranslationally attached to the carrier protein by a dedicated phosphopantetheine transferase. Introduction of pantetheine analogs into the co-enzyme A pathway can result in modified carrier protein in vitro and in vivo. We have previously reported the in vivo labeling of carrier proteins in overexpression systems, and the relation between an analogs kinetic profile with CoaA and its suitability for in vivo carrier protein modification. Here we expand this technique by demonstrating the in vivo labeling of carrier proteins in native systems. This technique allows for the detection of novel carrier proteins from many organisms without cloning or overexpression. It also provides a means with which to study the modification of ACP as a scaffold for fatty acid biosynthesis inhibitors. |
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Poster Session
8:00 PM-10:00 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |