Cellular Localization of Isoprenoid Biosynthetic Enzymes inMarchantia polymorpha. Uncovering a New Role of Oil Bodies
- 1 November 2000
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 124 (3) , 971-978
- https://doi.org/10.1104/pp.124.3.971
Abstract
Like seed plants, liverworts synthesize and accumulate a myriad of isoprenoid compounds. Using antibodies raised against several isoprenoid biosynthetic enzymes, we investigated their intracellular compartmentation by in situ immunolocalization from Marchantia polymorpha. The enzymes examined were deoxy-xylulose phosphate synthase, geranyl diphosphate synthase, farnesyl diphosphate synthase, geranylgeranyl diphosphate synthase, monoterpene synthase, geranylgeranyl diphosphate reductase, phytoene synthase, and phytoene desaturase. Our results show that liverwort oil bodies, which are organelles bound by a single unit membrane, possess isoprenoid biosynthetic enzymes similar to those found in plastids and the cytosol. We postulate that oil bodies play a dynamic role in cell metabolism in addition to their role as sites of essential oil accumulation and sequestration. The occurrence of such enzymes in different cellular compartments might be due to multiple targeting of gene products to various organelles.Keywords
This publication has 34 references indexed in Scilit:
- Characterization of the Contents of Oil Bodies from the Liverwort Radula complanata1Plant Biology, 2000
- ChloroP, a neural network‐based method for predicting chloroplast transit peptides and their cleavage sitesProtein Science, 1999
- Monoterpene Biosynthesis in the Liverwort Conocephalum Conicum: Demonstration of Sabinene Synthase and Bornyl Diphosphate Synthase in Honour of Professor G. H. Neil Towers 75th BirthdayPhytochemistry, 1998
- Truncation of Limonene Synthase Preprotein Provides a Fully Active ‘Pseudomature' Form of This Monoterpene Cyclase and Reveals the Function of the Amino-Terminal Arginine PairBiochemistry, 1998
- The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases.Plant Cell, 1996
- Intracellular localization of geranylpyrophosphate synthase from cell cultures of Lithospermum erythrorhizonPhytochemistry, 1995
- Biosynthesis of sesquiterpenes of cadinane type in cultured cells of Heteroscyphus planusPhytochemistry, 1994
- Characterization and molecular cloning of a flavoprotein catalyzing the synthesis of phytofluene and ζ‐carotene in Capsicum chromoplastsEuropean Journal of Biochemistry, 1992
- Purification of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthase from Capsicum chromoplasts by affinity chromatographyBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987
- 3,10-Dihydro-1,4-dimethylazulene, a labile biosynthetic intermediate isolated from cultured cells of liverwort Calypogeia granulata InoueJournal of the American Chemical Society, 1983