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J Biol Chem, Vol. 275, Issue 19, 14095-14101, May 12, 2000
From the The N-methylation of
phosphoethanolamine is the committing step in choline biogenesis in
plants and is catalyzed by
S-adenosyl-L-methionine:phosphoethanolamine N-methyltransferase (PEAMT, EC 2.1.1.103). A spinach
PEAMT cDNA was isolated by functional complementation of a
Schizosaccharomyces pombe cho2 The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF237633.
cDNA Cloning of Phosphoethanolamine
N-Methyltransferase from Spinach by Complementation in
Schizosaccharomyces pombe and Characterization of the
Recombinant Enzyme*
,,
Horticultural Sciences Department,
University of Florida, Gainesville, Florida 32611, the
§ Department of Biological Sciences, Carnegie Mellon
University, Pittsburgh, Pennsylvania 15213, and the ¶ Department
of Biology, McMaster University,
Hamilton, Ontario L8S 4K1, Canada
mutant and was
shown to encode a protein with PEAMT activity and without ethanolamine-
or phosphatidylethanolamine N-methyltransferase activity. The PEAMT cDNA specifies a 494-residue polypeptide
comprising two similar, tandem methyltransferase domains, implying that
PEAMT arose by gene duplication and fusion. Data base searches
suggested that PEAMTs with the same tandem structure are widespread
among flowering plants. Size exclusion chromatography of the
recombinant enzyme indicates that it exists as a monomer. PEAMT
catalyzes not only the first N-methylation of
phosphoethanolamine but also the two subsequent
N-methylations, yielding phosphocholine. Monomethyl- and
dimethylphosphoethanolamine are detected as reaction intermediates. A
truncated PEAMT lacking the C-terminal methyltransferase domain catalyzes only the first methylation. Phosphocholine inhibits both the
wild type and the truncated enzyme, although the latter is less
sensitive. Salinization of spinach plants increases PEAMT mRNA
abundance and enzyme activity in leaves by about 10-fold, consistent
with the high demand in stressed plants for choline to support glycine
betaine synthesis.
*
This work was supported in part by United States Department
of Agriculture-National Research Initiative-Competitive Grants Program
Grant 98-35100-6149 (to A. D. H.), by National Institutes of
Health Grant GM19629 (to S. A. H.), by an endowment from the C. V. Griffin, Sr. Foundation, and by the Florida Agricultural Experiment Station (Journal Series R-07329).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.
To whom correspondence should be addressed: Horticultural
Sciences Dept., University of Florida, P.O. Box 110690, Gainesville, FL
32611. Tel.: 352-392-1928; Fax: 352-392-6479; E-mail:
adha@gnv.ifas.ufl.edu.
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