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Plant Physiol, December 2000, Vol. 124, pp. 1800-1813
The Isolation and Characterization in Yeast of a Gene for
Arabidopsis S-Adenosylmethionine:Phospho-Ethanolamine
N-Methyltransferase1
Cynthia P.
Bolognese and
Patricia
McGraw*
Department of Biological Sciences, University of Maryland,
Baltimore, Maryland 21250
Saccharomyces cerevisiae opi3 mutant strains do not
have the phospholipid N-methyltransferase that catalyzes
the two terminal methylations in the phosphatidylcholine (PC)
biosynthetic pathway. This results in a build up of the intermediate
phosphatidylmonomethylethanolamine, causing a temperature-sensitive
growth phenotype. An Arabidopsis cDNA library was used to isolate three
overlapping plasmids that complemented the temperature-sensitive
phenotype. Phospholipid analysis showed that the presence of the cloned
cDNA caused a 65-fold reduction in the level of
phosphatidylmonomethylethanolamine and a significant, though not
equivalent, increase in the production of PC. Sequence analysis
established that the cDNA was not homologous to OPI3 or
to CHO2, the only other yeast phospholipid
N-methyltransferase, but was similar to several other
classes of methyltransferases. S-adenosyl-Met:phospho-base
N-methyltransferase assays revealed that the cDNA
catalyzed the three sequential methylations of phospho-ethanolamine to
form phospho-choline. Phospho-choline is converted to PC by the
CDP-choline pathway, explaining the phenotype conferred upon the yeast
mutant strain by the cDNA. In accordance with this the gene has been
named AtNMT1. The identification of this enzyme and the
failure to isolate a plant phospholipid
N-methyltransferase suggests that there are fundamental
differences between the pathways utilized by yeast and by some plants
for synthesis of PC.
1
This work was supported by the National Science
Foundation (grant no. MCB-9118355 to P.M.).
*
Corresponding author; e-mail mcgraw{at}umbc.edu; fax
410-455-3875.
© 2000 American Society of Plant Physiologists
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