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J. Biol. Chem., Vol. 275, Issue 25, 18919-18925, June 23, 2000
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From the Phosphatidylcholine (PC) is the major
membrane-forming phospholipid in eukaryotes and can be synthesized by
either of two pathways, the CDP-choline pathway or the methylation
pathway. In prokaryotes only the methylation pathway was thought to
occur. Recently, however, we could demonstrate (de Rudder, K. E. E., Sohlenkamp, C., and Geiger, O. (1999) J. Biol.
Chem. 274, 20011-20016) that a second pathway for
phosphatidylcholine biosynthesis exists in Sinorhizobium
(Rhizobium) meliloti involving a novel enzymatic activity,
phosphatidylcholine synthase, that condenses choline and
CDP-diacylglyceride in one step to form PC and CMP. Using a colony
autoradiography method we have isolated mutants of S. meliloti deficient in phosphatidylcholine synthase and which are no longer able to incorporate radiolabeled choline into PC.
Complementation of such mutants with a sinorhizobial cosmid gene bank,
subcloning of the complementing fragment, and sequencing of the
subclone led to the identification of a gene coding for a presumptive
CDP-alcohol phosphatidyltransferase. Amplification of this gene and its
expression in Escherichia coli demonstrates that it codes
for phosphatidylcholine synthase. Genomes of some pathogens
(Pseudomonas aeruginosa and Borrelia
burgdorferi) contain genes similar to the sinorhizobial gene
(pcs) for phosphatidylcholine synthase. Although
pcs-deficient S. meliloti knock-out mutants
show wild type-like growth and lipid composition, they are unable to
perform rapid PC biosynthesis that normally is achieved via the
phosphatidylcholine synthase pathway in S. meliloti wild type.
This article is dedicated to Eugene P. Kennedy on the occasion of his
80th birthday.
Cloning and Characterization of the Gene for Phosphatidylcholine
Synthase*
,,, Institute of Biotechnology, Technical
University of Berlin, Seestrasse 13, D-13353 Berlin, Germany and the
§ Centro de Investigación sobre Fijación de
Nitrógeno, Universidad Nacional Autónoma de México,
Apdo. Postal 565-A, Cuernavaca, Morelos, CP62210, México
*
This work was supported by the Deutsche
Forschungsgemeinschaft (Ge556/2-3).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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