Publications

• 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.

• Evolution of floral scent in Clarkia: novel patterns of S-linalool synthase gene expression in the C. breweri flower.

  Dudareva N., Cseke L., Blanc V.M., Pichersky E.

  Flowers of Clarkia breweri, an annual plant from the coastal range of California, emit a strong sweet scent of which S-linalool, an acyclic monoterpene, is a major component. Chromosomal, chemical, and morphological data, and the species' geographic distribution, suggest that C. breweri evolved fr ... >> More

  Flowers of Clarkia breweri, an annual plant from the coastal range of California, emit a strong sweet scent of which S-linalool, an acyclic monoterpene, is a major component. Chromosomal, chemical, and morphological data, and the species' geographic distribution, suggest that C. breweri evolved from an extant nonscented species, C. concinna. A cDNA of Lis, the gene encoding S-linalool synthase, was isolated from C. breweri. We show that in C. breweri, Lis is highly expressed in cells of the transmitting tract of the stigma and style and in the epidermal cells of petals, as well as in stamens, whereas in the nonscented C. concinna, Lis is expressed only in the stigma and at a relatively low level. In both species, changes in protein levels parallel changes in mRNA levels, and changes in enzyme activity levels parallel changes in protein levels. The results indicate that in C. breweri, the expression of Lis has been upregulated and its range enlarged to include cells not expressing this gene in C. concinna. These results show how scent can evolve in a relatively simple way without the evolution of highly specialized "scent glands" and other specialized structures. Lis encodes a protein that is structurally related to the family of proteins termed terpene synthases. The protein encoded by Lis is the first member of this family found to catalyze the formation of an acyclic monoterpene. << Less

  Plant Cell 8:1137-1148(1996) [PubMed] [EuropePMC]

• Expression of Clarkia S-linalool synthase in transgenic petunia plants results in the accumulation of S-linalyl-beta-D-glucopyranoside.

  Lucker J., Bouwmeester H.J., Schwab W., Blaas J., van der Plas L.H., Verhoeven H.A.

  Petunia hybrida W115 was transformed with a Clarkia breweri S-linalool synthase cDNA (lis). Lis was expressed in all tissues analysed, and linalool was detected in leaves, sepals, corolla, stem and ovary, but not in nectaries, roots, pollen and style. However, the S-linalool produced by the plant ... >> More

  Petunia hybrida W115 was transformed with a Clarkia breweri S-linalool synthase cDNA (lis). Lis was expressed in all tissues analysed, and linalool was detected in leaves, sepals, corolla, stem and ovary, but not in nectaries, roots, pollen and style. However, the S-linalool produced by the plant in the various tissues is not present as free linalool, but was efficiently converted to non-volatile S-linalyl-beta-D-glucopyranoside by the action of endogenous glucosyltransferase. The results presented demonstrate that monoterpene production can be altered by genetic modification, and that the compounds produced can be converted by endogenous enzymatic activity. << Less

  Plant J 27:315-324(2001) [PubMed] [EuropePMC]

• Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri.

  Pichersky E., Lewinsohn E., Croteau R.

  S-Linalool is one of the volatiles emitted by Clarkia breweri Grey [Green] flowers to attract its moth pollinator. S-Linalool synthase, the enzyme that stereoselectively converts the ubiquitous C10 intermediate GPP to S-linalool, is abundant in stigmata of freshly opened flowers, and it was purifi ... >> More

  S-Linalool is one of the volatiles emitted by Clarkia breweri Grey [Green] flowers to attract its moth pollinator. S-Linalool synthase, the enzyme that stereoselectively converts the ubiquitous C10 intermediate GPP to S-linalool, is abundant in stigmata of freshly opened flowers, and it was purified to > 95% homogeneity by anion-exchange and hydroxyapatite chromatography. S-Linalool synthase is operationally soluble as are other monoterpene synthases, has a Km of 0.9 microM for geranyl pyrophosphate, exhibits a strict requirement for a divalent metal cofactor with a preference for Mn2+ (Km = 45 microM), and shows an optimal pH of 7.4. The enzyme is active as a monomer of 76 +/-3 kDa as determined by gel permeation chromatography and polyacrylamide gel electrophoresis. Neither S-nor R-linalyl pyrophosphates are substrates for the C. breweri S-linalool synthase, although this tertiary allylic pyrophosphate ester is a bound intermediate in the biosynthesis of cyclic monoterpenes from geranyl pyrophosphate in many plant species, where it also serves as an alternate substrate. << Less

  Arch Biochem Biophys 316:803-807(1995) [PubMed] [EuropePMC]