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Oleosin Is Bifunctional Enzyme That Has Both Monoacylglycerol Acyltransferase and Phospholipase Activities

Parthibane, Velayoudame and Rajakumari, Sona and Venkateshwari, Varadarajan and Iyappan, Ramachandiran and Rajasekharan, Ram (2012) Oleosin Is Bifunctional Enzyme That Has Both Monoacylglycerol Acyltransferase and Phospholipase Activities. In: Journal of Biological Chemistry, 287 (3). pp. 1946-1954.

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Official URL: http://www.jbc.org/content/287/3/1946.abstract


In plants, fatty oils are generally stored in spherical intracellular organelles referred to as oleosomes that are covered by proteins such as oleosin. Seeds with high oil content have more oleosin than those with low oil content. However, the exact role of oleosin in oil accumulation is thus far unclear. Here, we report the isolation of a catalytically active 14 S multiprotein complex capable of acylating monoacylglycerol from the microsomal membranes of developing peanut cotyledons. Microsomal membranes from immature peanut seeds were solubilized using 8 M urea and 10 mM CHAPS. Using two-dimensional gel electrophoresis and mass spectrometry, we identified 27 proteins in the 14 S complex. The major proteins present in the 14 S complex are conarachin, the major allergen Ara h 1, and other seed storage proteins. We identified oleosin 3 as a part of the 14 S complex, which is capable of acylating monoacylglycerol. The recombinant OLE3 microsomes from Saccharomyces cerevisiae have been shown to have both a monoacylglycerol acyltransferase and a phospholipase A(2) activity. Overexpression of the oleosin 3 (OLE3) gene in S. cerevisiae resulted in an increased accumulation of diacylglycerols and triacylglycerols and decreased phospholipids. These findings provide a direct role for a structural protein (OLE3) in the biosynthesis and mobilization of plant oils.

Item Type: Journal Article
Publication: Journal of Biological Chemistry
Publisher: The American Society for Biochemistry and Molecular Biology
Additional Information: Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 21 Feb 2012 07:13
Last Modified: 21 Feb 2012 07:13
URI: http://eprints.iisc.ac.in/id/eprint/43528

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