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Plant Cell, Vol. 11, 1485-1498, August 1999, Copyright © 1999, American Society of Plant Physiologists

S-Methylmethionine Plays a Major Role in Phloem Sulfur Transport and Is Synthesized by a Novel Type of Methyltransferase

Fabienne Bourgisa, Sanja Rojea, Michael L. Nuccioa, Donald B. Fisherb, Mitchell C. Tarczynskic, Changjiang Lic, Cornelia Herschbachd, Heinz Rennenbergd, Maria Joao Pimentae, Tun-Li Shenf, Douglas A. Gagef, and Andrew D. Hansona
a Horticultural Sciences Department, University of Florida, Gainesville, Florida 32611-0690
b Botany Department, Washington State University, Pullman, Washington 99164-4238
c Pioneer Hi-Bred International, 7300 N.W. 62nd Avenue, Johnston, Iowa 50131-1004
d Institut für Forstbotanik und Baumphysiologie, Albert-Ludwigs-Universität, D-79085 Freiburg, Germany
e Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan
f Biochemistry Department, Michigan State University, East Lansing, Michigan 48824-1319

Correspondence to: Andrew D. Hanson, adha{at}gnv.ifas.ufl.edu (E-mail), 352-392-6479 (fax)

All flowering plants produce S-methylmethionine (SMM) from Met and have a separate mechanism to convert SMM back to Met. The functions of SMM and the reasons for its interconversion with Met are not known. In this study, by using the aphid stylet collection method together with mass spectral and radiolabeling analyses, we established that L-SMM is a major constituent of the phloem sap moving to wheat ears. The SMM level in the phloem (~2% of free amino acids) was 1.5-fold that of glutathione, indicating that SMM could contribute approximately half the sulfur needed for grain protein synthesis. Similarly, L-SMM was a prominently labeled product in phloem exudates obtained by EDTA treatment of detached leaves from plants of the Poaceae, Fabaceae, Asteraceae, Brassicaceae, and Cucurbitaceae that were given L–35S-Met. cDNA clones for the enzyme that catalyzes SMM synthesis (S-adenosylMet:Met S-methyltransferase; EC 2.1.1.12) were isolated from Wollastonia biflora, maize, and Arabidopsis. The deduced amino acid sequences revealed the expected methyltransferase domain (~300 residues at the N terminus), plus an 800-residue C-terminal region sharing significant similarity with aminotransferases and other pyridoxal 5'-phosphate–dependent enzymes. These results indicate that SMM has a previously unrecognized but often major role in sulfur transport in flowering plants and that evolution of SMM synthesis in this group involved a gene fusion event. The resulting bipartite enzyme is unlike any other known methyltransferase.




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