NEW PATHWAY TO POLYKETIDES IN PLANTS

The repertoire of secondary metabolism (involving the production of co mpounds not essential for growth) in the plant kingdom is enormous, bu t the genetic and functional basis for this diversity is hard to analy se as many of the biosynthetic enzymes are unknown. We have now identi fied a key enzyme in the ornamental plant Gerbera hybrida (Asteraceae) that participates in the biosynthesis of compounds that contribute to insect and pathogen resistance. Plants transformed with an antisense construct of gchs2, a complementary DNA encoding a previously unknown function(1,2), completely lack the pyrone derivatives gerberin and par asorboside. The recombinant plant protein catalyses the principal reac tion in the biosynthesis of these derivatives: GCHS2 is a polyketide s ynthase that uses acetyl-CoA and two condensation reactions with malon yl-CoA to form the pyrone backbone of the natural products. The enzyme also accepts benzoyl-CoA to synthesize the backbone of substances tha t have become of interest as inhibitors of the HIV-1 protease(3-5). GC HS2 is related to chalcone synthase (CHS) and its properties define a new class of function in the protein superfamily. It appears that CHS- related enzymes are involved in the biosynthesis of a much larger rang e of plant products than was previously realized.