Publications

• An unusual skeletal rearrangement in the biosynthesis of the sesquiterpene trichobrasilenol from Trichoderma.

  Murai K., Lauterbach L., Teramoto K., Quan Z., Barra L., Yamamoto T., Nonaka K., Shiomi K., Nishiyama M., Kuzuyama T., Dickschat J.S.

  The skeletons of some classes of terpenoids are unusual in that they contain a larger number of Me groups (or their biosynthetic equivalents such as olefinic methylene groups, hydroxymethyl groups, aldehydes, or carboxylic acids and their derivatives) than provided by their oligoprenyl diphosphate ... >> More

  The skeletons of some classes of terpenoids are unusual in that they contain a larger number of Me groups (or their biosynthetic equivalents such as olefinic methylene groups, hydroxymethyl groups, aldehydes, or carboxylic acids and their derivatives) than provided by their oligoprenyl diphosphate precursor. This is sometimes the result of an oxidative ring-opening reaction at a terpene-cyclase-derived molecule containing the regular number of Me group equivalents, as observed for picrotoxan sesquiterpenes. In this study a sesquiterpene cyclase from Trichoderma spp. is described that can convert farnesyl diphosphate (FPP) directly via a remarkable skeletal rearrangement into trichobrasilenol, a new brasilane sesquiterpene with one additional Me group equivalent compared to FPP. A mechanistic hypothesis for the formation of the brasilane skeleton is supported by extensive isotopic labelling studies. << Less

  Angew. Chem. Int. Ed. 58:15046-15050(2019) [PubMed] [EuropePMC]

  This publication is cited by 7 other entries.

• Nonseed plant Selaginella moellendorfii has both seed plant and microbial types of terpene synthases.

  Li G., Kollner T.G., Yin Y., Jiang Y., Chen H., Xu Y., Gershenzon J., Pichersky E., Chen F.

  Terpene synthases (TPSs) are pivotal enzymes for the biosynthesis of terpenoids, the largest class of secondary metabolites made by plants and other organisms. To understand the basis of the vast diversification of these enzymes in plants, we investigated Selaginella moellendorffi, [corrected] a n ... >> More

  Terpene synthases (TPSs) are pivotal enzymes for the biosynthesis of terpenoids, the largest class of secondary metabolites made by plants and other organisms. To understand the basis of the vast diversification of these enzymes in plants, we investigated Selaginella moellendorffi, [corrected] a nonseed vascular plant. The genome of this species was found to contain two distinct types of TPS genes. The first type of genes, which was designated as S. moellendorffi [corrected] TPS genes (SmTPSs), consists of 18 members. SmTPSs share common ancestry with typical seed plant TPSs. Selected members of the SmTPSs were shown to encode diterpene synthases. The second type of genes, designated as S. moellendorffi [corrected] microbial TPS-like genes (SmMTPSLs), consists of 48 members. Phylogenetic analysis showed that SmMTPSLs are more closely related to microbial TPSs than other plant TPSs. Selected SmMTPSLs were determined to function as monoterpene and sesquiterpene synthases. Most of the products formed were typical monoterpenes and sesquiterpenes that have been previously shown to be synthesized by classical plant TPS enzymes. Some in vitro products of the characterized SmMTPSLs were detected in the headspace of S. moellendorffi [corrected] plants treated with the fungal elicitor alamethicin, showing that they are also formed in the intact plant. The presence of two distinct types of TPSs in the genome of S. moellendorffi [corrected] raises the possibility that the TPSs in other plant species may also have more than one evolutionary origin. << Less

  Proc. Natl. Acad. Sci. U.S.A. 109:14711-14715(2012) [PubMed] [EuropePMC]

  This publication is cited by 4 other entries.

• Diversity and Functional Evolution of Terpene Synthases in Dictyostelid Social Amoebae.

  Chen X., Kollner T.G., Shaulsky G., Jia Q., Dickschat J.S., Gershenzon J., Chen F.

  Dictyostelids, or social amoebae, have a unique life style in forming multicellular fruiting bodies from unicellular amoeboids upon starvation. Recently, dictyostelids were found to contain terpene synthase (TPS) genes, a gene type of secondary metabolism previously known to occur only in plants, ... >> More

  Dictyostelids, or social amoebae, have a unique life style in forming multicellular fruiting bodies from unicellular amoeboids upon starvation. Recently, dictyostelids were found to contain terpene synthase (TPS) genes, a gene type of secondary metabolism previously known to occur only in plants, fungi and bacteria. Here we report an evolutionary functional study of dictyostelid TPS genes. The number of TPS genes in six species of dictyostelids examined ranges from 1 to 19; and the model species Dictyostelium purpureum contains 12 genes. Using in vitro enzyme assays, the 12 TPS genes from D. purpureum were shown to encode functional enzymes with distinct product profiles. The expression of the 12 TPS genes in D. purpureum is developmentally regulated. During multicellular development, D. purpureum releases a mixture of volatile terpenes dominated by sesquiterpenes that are the in vitro products of a subset of the 12 TPS genes. The quality and quantity of the terpenes released from D. purpureum, however, bear little resemblance to those of D. discoideum, a closely related dictyostelid. Despite these variations, the conserved clade of dictyostelid TPSs, which have an evolutionary distance of more than 600 million years, has the same biochemical function, catalyzing the formation of a sesquiterpene protoillud-7-ene. Taken together, our results indicate that the dynamic evolution of dictyostelid TPS genes includes both purifying selection of an orthologous group and species-specific expansion with functional divergence. Consequently, the terpenes produced by these TPSs most likely have conserved as well as species-adaptive biological functions as chemical languages in dictyostelids. << Less

  Sci. Rep. 8:14361-14361(2018) [PubMed] [EuropePMC]

  This publication is cited by 6 other entries.