2000 Volume 17 Issue 3 Pages 203-210
The genes encoding chalcone synthase (CHS) in the common morning glory (Ipomoea purpurea) comprise a multigene family, and they are divided into two subfamilies. The genes in a subfamily including the CHS-A, CHS-B and CHS-C genes are distantly related to the other known CHS sequences in a phylogenetic tree, whereas the CHS-D and CHS-E genes in another subfamily are more closely related to the well-characterized CHS genes.
As an initial step to elucidate biological function of these CHS genes in I. purpurea, the CHS-D and CHS-E cDNAs were expressed in Escherichia coli with different expression systems. The recombinant CHS-D and CHS-E proteins both showed CHS activity to produce naringenin chalcone. These results are discussed with regard to the biological roles of the CHS-D and CHS-E genes in flower pigmentation in I. purpurea. We have also discussed these CHS-D and CHS-E enzyme as members of plant specific polyketide synthases.
