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Originally published In Press as doi:10.1074/jbc.M001116200 on March 21, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15962-15968, May 26, 2000
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Characterization and Functional Expression of cDNAs Encoding Methionine-sensitive and -insensitive Homocysteine S-Methyltransferases from Arabidopsis*

Philippe RanochaDagger , Fabienne BourgisDagger , Michael J. ZiemakDagger , David Rhodes§, Douglas A. Gage, and Andrew D. HansonDagger ||

From the Dagger  Horticultural Sciences Department, University of Florida, Gainesville, Florida 32611, the § Department of Horticulture, Purdue University, West Lafayette, Indiana 47907, and the  Biochemistry Department, Michigan State University, East Lansing, Michigan 48824

Plants synthesize S-methylmethionine (SMM) from S-adenosylmethionine (AdoMet), and methionine (Met) by a unique reaction and, like other organisms, use SMM as a methyl donor for Met synthesis from homocysteine (Hcy). These reactions comprise the SMM cycle. Two Arabidopsis cDNAs specifying enzymes that mediate the SMM right-arrow Met reaction (SMM:Hcy S-methyltransferase, HMT) were identified by homology and authenticated by complementing an Escherichia coli yagD mutant and by detecting HMT activity in complemented cells. Gel blot analyses indicate that these enzymes, AtHMT-1 and -2, are encoded by single copy genes. The deduced polypeptides are similar in size (36 kDa), share a zinc-binding motif, lack obvious targeting sequences, and are 55% identical to each other. The recombinant enzymes exist as monomers. AtHMT-1 and -2 both utilize L-SMM or (S,S)-AdoMet as a methyl donor in vitro and have higher affinities for SMM. Both enzymes also use either methyl donor in vivo because both restore the ability to utilize AdoMet or SMM to a yeast HMT mutant. However, AtHMT-1 is strongly inhibited by Met, whereas AtHMT-2 is not, a difference that could be crucial to the control of flux through the HMT reaction and the SMM cycle. Plant HMT is known to transfer the pro-R methyl group of SMM. This enabled us to use recombinant AtHMT-1 to establish that the other enzyme of the SMM cycle, AdoMet:Met S-methyltransferase, introduces the pro-S methyl group. These opposing stereoselectivities suggest a way to measure in vivo flux through the SMM cycle.

* This work was supported in part by National Science Foundation Grants IBN-9816075 (to A. D. H) and IBN-9904263 (to D. A. G.), by Department of Energy Grant DE-FG02-99ER20344 (to D. R.), by an endowment from the C. V. Griffin, Sr. Foundation, and by the Florida Agricultural Experiment Station. Journal series no. R-07506.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF219222 (AtHMT-1) and AF219223 (AtHMT-2).

|| 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.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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