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Two Enzymes of Diacylglyceryl-O-4′-(N,N,N,-Trimethyl)-Homoserine Biosynthesis Are Encoded by btaA and btaB in the Purple Bacterium Rhodobacter sphaeroides
Rouven M. Klug and Christoph Benning
Proceedings of the National Academy of Sciences of the United States of America
Vol. 98, No. 10 (May 8, 2001), pp. 5910-5915
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3055726
Page Count: 6
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Betaine lipids are ether-linked, nonphosphorous glycerolipids that resemble the more commonly known phosphatidylcholine in overall structure. Betaine lipids are abundant in many eukaryotes such as nonseed plants, algae, fungi, and amoeba. Some of these organisms are entirely devoid of phosphatidylcholine and, instead, contain a betaine lipid such as diacylglyceryl-O-4′-(N,N,N,-trimethyl)homoserine. Recently, this lipid also was discovered in the photosynthetic purple bacterium Rhodobacter sphaeroides where it seems to replace phosphatidylcholine under phosphate-limiting growth conditions. This discovery provided the opportunity to study the biosynthesis of betaine lipids in a bacterial model system. Mutants of R. sphaeroides deficient in the biosynthesis of the betaine lipid were isolated, and two genes essential for this process, btaA and btaB, were identified. It is proposed that btaA encodes an S-adenosylmethionine:diacylglycerol 3-amino-3-carboxypropyl transferase and btaB an S-adenosylmethionine-dependent N-methyltransferase. Both enzymatic activities can account for all reactions of betaine lipid head group biosynthesis. Because the equivalent reactions have been proposed for different eukaryotes, it seems likely that orthologs of btaA/btaB may be present in other betaine lipid-containing organisms.
Proceedings of the National Academy of Sciences of the United States of America © 2001 National Academy of Sciences