ibclogo XVI International Botanical Congess


Abstract Number: 2853
Poster No. = 2115


ISOPRENOID BIOSYNTHESIS IN THE SAGEBRUSH ARTEMISIA TRIDENTATA SPICIFORMIS: ISOLATION OF FARNESYL DIPHOSPHATE SYNTHASE LIKE cDNAS


Andréa Hemmerlin and C. Dale Poulter University of Utah, Chemistry Department


In plants, isoprenoid compounds represent a large and structurally diverse family that are implicated in primary and secondary metabolism. Several enzymes implicated in the biosynthetic pathway are coded by gene families. Consequently, in contrast to other higher eukaryotic cells, it is common to have several different enzyme isoforms. One enzyme is farnesyl diphosphate (FPP) synthase (FPS), a key enzyme which catalyzes the formation of FPP from IPP and DMAPP. Using degenerate primers specific to FPS motifs (DDXXD), we amplified from the sagebrush PCR products. Four different DNA fragments have been identified as having similarity with other FPSs. In order to characterize the corresponding enzymes, isolation of the full-length cDNAs and subcloning into E. coli expression vectors has been investigated.


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