You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
CYP86B1 Is Required for Very Long Chain ω-Hydroxyacid and α,ω-Dicarboxylic Acid Synthesis in Root and Seed Suberin Polyester
Vincent Compagnon, Patrik Diehl, Irène Benveniste, Denise Meyer, Hubert Schaller, Lukas Schreiber, Rochus Franke and Franck Pinot
Vol. 150, No. 4 (Aug., 2009), pp. 1831-1843
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/40537899
Page Count: 13
You can always find the topics here!Topics: Fatty acids, Plants, Plant roots, Testa, Polyesters, Monomers, Cytochromes, Biosynthesis, Guard cells, Lipids
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Suberin composition of various plants including Arabidopsis (Arabidopsis thaliana) has shown the presence of very long chain fatty acid derivatives C20 in addition to the C16 and C18 series. Phylogenetic studies and plant genome mining have led to the identification of putative aliphatic hydroxylases belonging to the CYP86B subfamily of cytochrome P450 monooxygenases. In Arabidopsis, this subfamily is represented by CYP86B1 and CYP86B2, which share about 45% identity with CYP86A1, a fatty acid cü-hydroxylase implicated in root suberin monomer synthesis. Here, we show that CYP86B1 is located to the endoplasmic reticulum and is highly expressed in roots. Indeed, CYP86B1 promoter-driven jS-glucuronidase expression indicated strong reporter activities at known sites of suberin production such as the endodermis. These observations, together with the fact that proteins of the CYP86B type are widespread among plant species, suggested a role of CYP86B1 in suberin biogenesis. To investigate the involvement of CYP86B1 in suberin biogenesis, we characterized an allelic series of cyp86Bl mutants of which two strong alleles were knockouts and two weak ones were RNA interference-silenced lines. TÏiese root aliphatic plant hydroxylase lines had a root and a seed coat aliphatic polyester composition in which C22-and C24-hydroxyacids and a, o)-dicarboxylic acids were strongly reduced. However, these changes did not affect seed coat permeability and ion content in leaves. The presumed precursors, C22 and C24 fatty acids, accumulated in the suberin polyester. These results demonstrate that CYP86B1 is a very long chain fatty acid hydroxylase specifically involved in polyester monomer biosynthesis during the course of plant development.
Plant Physiology © 2009 American Society of Plant Biologists (ASPB)