Diversity in KCS2 (Ketoacyl-CoA Synthase) of selected plants and its molecular implications: A computational analysis
231 / 73
Keywords:
Acyl-CoA, Fatty acids, KCS2, ProteinsAbstract
The majority of calories in human food are derived from plant fatty acids. Besides,plant fatty acids are also a major component of a variety of products useful to human beings such as paints, cosmetics, biofuels, lubricants, detergents and soaps. Ketoacyl-CoA synthase is a key enzyme involved in the fatty acid elongation in plants In this study, we have analyzed the diversity in the KCS2 proteins of a selected plant species. We conclude that though there are extensive similarities in the KCS2 proteins studied with respect to total number of negatively charged residues, total number of positively charged residues, and domain organization, there are notable differences for other features such as extinction coefficients, protein stability, kinase specific phosphorylation sites, number of O-GlcNAc sites, predicted sumoylation sites, residues contributing to nuclear export signal and transmemebrane helices. These differences may have repercussions for the quantitative efficiency of the 3-Ketoacyl-CoA synthase enzyme which catalyzes the condensation of c2 units to acyl coA during the fatty acid elongation process, and its regulation. This paper showcases molecular implications of diversity in KCS2 , which can be used to create a diverse genetic base for engineering KCS 2 genes.Downloads
References
Broun P, Gettner S and Somerville C. 1999. Genetic engineering of plant lipids. Annual Review Nutrition. 19: 197–216. DOI: https://doi.org/10.1146/annurev.nutr.19.1.197
Ohlrogge J B. 1994. Design of new plant products: Engineering of fatty acid metabolism. Plant Physiology 104 : 821–6. DOI: https://doi.org/10.1104/pp.104.3.821
Voelker T and Kinney A. 2001. Variations in the biosynthesis of seed storage lipids. Annual Review Plant Physiology and Plant Molecular Biology 52: 335–361 DOI: https://doi.org/10.1146/annurev.arplant.52.1.335
Schneiter R, Hitomi, M, Ivessa A S, Fasch E V, Kohlwein S P and Tartakoff M. 1996. A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Molecular Cell Biology 16: 7 161–72. DOI: https://doi.org/10.1128/MCB.16.12.7161
Devaiah S P, Roth M R, Baughman E, Li M, Tamura P, Jeannotte R, Welti R. and Wang X. 2006. Quantitative profiling of polar glycerolipid species from organs of wild-type Arabidopsis and a phospholipase D 1 knockout mutant. Phytochemistry 67: 1 907–24. DOI: https://doi.org/10.1016/j.phytochem.2006.06.005
Dickson R C, Sumanasekera C and Lester R L. 2006. Functions and metabolism of sphingolipids in Saccharomyces cerevisiae. Prog. Lipid Research 45: 447–65. DOI: https://doi.org/10.1016/j.plipres.2006.03.004
Stefansson B R, Hougen E W and Downey R K. 1961. Note on the isolation of rape plants with seed oil free from erucic acid. Canadian Journal of Plant Science 41: 218–9. DOI: https://doi.org/10.4141/cjps61-028
Lassner M W. Lardizabal K and Metz J G. 1996. A jojoba β-ketoacyl-CoA synthase cDNA complements the canola fatty acid elongation mutation in transgenic plants. Plant Cell 8: 281–92. DOI: https://doi.org/10.1105/tpc.8.2.281
Barret P, Delourne R, Renard M, Domergue F, Lessire R, Delseny M and Roscoe T J. 1998. A rapeseed FAE1 gene is linked to the E1 locus associated with variation in the content of erucic acid. Theoretical Applied Genetics. 96: 177–86. DOI: https://doi.org/10.1007/s001220050725
Kolattukudy P E. 2001. Polyesters in higher plants. Advances Biochemical Engineering Biotechnology. 71: 1–49. DOI: https://doi.org/10.1007/3-540-40021-4_1
Bernards M A. 2002. Demystifying suberin. Canadian Journal of Botany 80: 227–40. DOI: https://doi.org/10.1139/b02-017
Franke R and Schreiber L. 2007. Suberin – a biopolyester forming apoplastic plant interfaces. Current Opinion in Plant Biology 10: 252–9. DOI: https://doi.org/10.1016/j.pbi.2007.04.004
Pollard M, Beisson F, Li Y and Ohlrogge J B. 2008. Building lipid barriers: biosynthesis of cutin and suberin. Trends in Plant Science 13: 236–46. DOI: https://doi.org/10.1016/j.tplants.2008.03.003
Post-Beittenmiller D. 1996. Biochemistry and molecular biology of wax production in plants. Annual Review Plant Physiology and Plant Molecular Biology. 47: 405–30. DOI: https://doi.org/10.1146/annurev.arplant.47.1.405
Kunst L and Samuels A L. 2003. Biosynthesis and secretion of plant cuticular wax. Prog. Lipid Research. 42: 51–80.
Samuels L, Kunst L and Jetter R. 2008. Sealing plant surfaces: cuticular wax formation by epidermal cells. Annual Review of Plant Biology. 59: 683–707. DOI: https://doi.org/10.1146/annurev.arplant.59.103006.093219
Reicosky D A and Hanover J W. 1978. Physiological effects of surface waxes. I. Light reflectance for glaucous and non- glaucous Picea pungens. Plant Physiology 62: 101–4. DOI: https://doi.org/10.1104/pp.62.1.101
Barthlott W and Neinhuis C. 1997. Purity of the sacred lotus, or escape from contamination in biological surfaces. Planta 202: 1–8. DOI: https://doi.org/10.1007/s004250050096
Kunst L and Samuels A L. 2003. Biosynthesis and secretion of plant cuticular wax. Prog. Lipid Research 42: 51–80. DOI: https://doi.org/10.1016/S0163-7827(02)00045-0
Beisson F, Koo A J K, Ruuska S et al. 2003. Arabidopsis genes involved in acyl lipid metabolism. A 2003 census of the candidates, a study of the distribution of expressed sequence tags in organs, and a web-based database. Plant Physiology 132: 681–97. DOI: https://doi.org/10.1104/pp.103.022988
Franke R, Höfer R, Briesen I, Emsermann M, Efremova N, Yephremov A and Schreiber L. 2009. The DAISY gene from Arabidopsis encodes a fatty acid elongase condensing enzyme involved in the biosynthesis of aliphatic suberin in roots and the chalaza–micropyle region of seeds. Plant Journal 57: 80–95. DOI: https://doi.org/10.1111/j.1365-313X.2008.03674.x
Lee S B, Jung S J, Go Y S, Kim H U, Kim J K, Cho H J, Park O K and Suh M C. 2009. Two Arabidopsis 3-ketoacyl CoA synthase genes, KCS20 and KCS2/DAISY, are functionally redundant in cuticular wax and root suberin biosynthesis, but differentially controlled by osmotic stress. Plant Journal 60: 462–75. DOI: https://doi.org/10.1111/j.1365-313X.2009.03973.x
Lis H and Sharon N. 1993. Protein glycosylation: Structural and functional aspects. Current Journal of Biochemistry 218: 1–27. DOI: https://doi.org/10.1111/j.1432-1033.1993.tb18347.x
Hounsell E F, Davies M J and Renouf D V. 1996. Olinked protein glycosylation structure and function. Glycoconjugate Journal 13: 19–26. DOI: https://doi.org/10.1007/BF01049675
Blom N, Gammeltoft S and Brunak S. 1999. Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. Journal of Molecular Biology 294(5): 1 351–62. DOI: https://doi.org/10.1006/jmbi.1999.3310
Fernández-Lloris R, Osses N, Jaffray E, Shen LN, Vaughan OA, Girwood D, Bartrons R, Rosa J L, Hay R T, Ventura F. 2006. Repression of SOX6 transcriptional activity by SUMO modification. FEBS Letters 580(5): 1 215–21. DOI: https://doi.org/10.1016/j.febslet.2006.01.031
Downloads
Submitted
Published
Issue
Section
License
Copyright (c) 2014 The Indian Journal of Agricultural Sciences

This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
The copyright of the articles published in The Indian Journal of Agricultural Sciences is vested with the Indian Council of Agricultural Research, which reserves the right to enter into any agreement with any organization in India or abroad, for reprography, photocopying, storage and dissemination of information. The Council has no objection to using the material, provided the information is not being utilized for commercial purposes and wherever the information is being used, proper credit is given to ICAR.