A root-specific condensing enzyme from Lesquerella fendleri that elongates very-long-chain saturated fatty acids
- 1 December 2004
- journal article
- research article
- Published by Springer Nature in Plant Molecular Biology
- Vol. 56 (6) , 917-927
Abstract
The LfKCS45 gene with a high sequence similarity to known 3-ketoacyl-CoA synthases of the membrane-bound fatty acid elongase was isolated from Lesquerella fendleri. The LfKCS45 gene has a 1464 bp open reading frame without introns, and is predicted to encode a polypeptide of 487 amino acids with an estimated molecular mass of 54.6 kD. High-stringency DNA blot analysis indicated that there were no closely related genes to LfKCS45 in the L. fendleri genome. Analysis of the fatty acid composition of transformed yeast revealed that expression of the LfKCS45 protein results in the synthesis of two novel very-long-chain fatty acids identified as C28:0 and C30:0. LfKCS45 was found to be not active with acyl-CoA substrates C16 to C24 in length. Reverse transcription-PCR experiments showed that the LfKCS45 gene is expressed only in L. fendleri root tips. Histochemical assays for GUS activity in Arabidopsis transformed with the LfKCS45 promoter-GUS fusion construct confirmed this expression pattern and demonstrated that LfKCS45 transcription is restricted to the cells of the lateral root cap.Keywords
This publication has 34 references indexed in Scilit:
- A Saccharomyces cerevisiae Gene Required for Heterologous Fatty Acid Elongase Activity Encodes a Microsomal β-Keto-reductaseJournal of Biological Chemistry, 2002
- The Endoplasmic Reticulum-Associated Maize GL8 Protein Is a Component of the Acyl-Coenzyme A Elongase Involved in the Production of Cuticular WaxesPlant Physiology, 2002
- A Condensing Enzyme from the Seeds of Lesquerella fendleri That Specifically Elongates Hydroxy Fatty AcidsPlant Physiology, 2001
- Active-site residues of a plant membrane-bound fatty acid elongase β-ketoacyl-CoA synthase, FAE1 KCSBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2001
- Biochemical and molecular characterization of corn (Zeo mays L.) root elongasesBiochemical Society Transactions, 2000
- Alterations in CER6, a Gene Identical to CUT1, Differentially Affect Long-Chain Lipid Content on the Surface of Pollen and StemsThe Plant Cell, 2000
- KCS1encodes a fatty acid elongase 3‐ketoacyl‐CoA synthase affecting wax biosynthesis inArabidopsis thalianaThe Plant Journal, 1999
- The Electronic Plant Gene RegisterPlant Physiology, 1997
- Acyl-CoA elongase from a higher plant (Lunaria annua): metabolic intermediates of very-long-chain acyl-CoA products and substrate specificityBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1991
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976