Bowerman, Pete A. , Winkel, Brenda S. J. .
Elucidation of the structure and architecture of the flavonoid multi-enzyme complex.
A key aspect of cellular metabolism is the assembly of biosynthetic enzymes into macromolecular complexes. Our lab utilizes the flavonoid biosynthetic pathway in the plant Arabidopsis thaliana as a model for understanding the structural and functional aspects of this organization. Flavonoids are involved in a variety of functions within the plant, including UV protection and auxin transport, and are also of considerable interest for their phytonutrient and pharmaceutical properties. A number of in vitro experiments have provided evidence for the interaction of several specific flavonoid enzymes. Some of this evidence indicates that these interacting enzymes form metabolic multi-enzyme complexes. These complexes offer a number of potential advantages to the cell, including channeling of toxic intermediates and rapid catalysis of several sequential reactions. My research interests center around understanding the structural architecture of these multi-enzyme metabolic complexes. A number of different approaches are being used, including using Tandem Affinity Purification (TAP-tagging) to isolate complexes that exist in planta. This method involves insertion of affinity tagged flavonoid enzymes in a null background, followed by isolation and identification of interacting proteins. In complementary experiments, chemical crosslinking followed by mass spectrometry analysis is being used to map the interaction interfaces of a number of flavonoid enzymes. In addition, biophysical approaches such as NMR are being explored as a means to further characterize the overall architecture of the flavonoid metabolon.
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1 - Virginia Tech, Biological Sciences, 432 Latham Hall, Ag Quad Lane, Blacksburg, VA, 24061, USA
2 - Virginia Tech, Biological Sciences
Presentation Type: Plant Biology Abstract
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM