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Plant Physiology 83:354-359 (1987)
© 1987 American Society of Plant Biologists

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Molecular Biology and Gene Regulation

Changes in the Levels of Major Sulfur Metabolites and Free Amino Acids in Pea Cotyledons Recovering from Sulfur Deficiency

Peter K. Macnicol and Peter J. Randall

Division of Plant Industry, Commonwealth Scientific and Industrial Research Organization, Canberra, A.C.T. 2601, Australia

Changes in levels of sulfur metabolites and free amino acids were followed in cotyledons of sulfur-deficient, developing pea seeds (Pisum sativum L.) for 24 hours after resupply of sulfate, during which time the legumin mRNA levels returned almost to normal. Two recovery situations were studied: cultured seeds, with sulfate added to the medium, and seeds attached to the intact plant, with sulfate added to the roots. In both situations the levels of cysteine, glutathione, and methionine rose rapidly, glutathione exhibiting an initial lag. In attached but not cultured seeds methionine markedly overshot the level normally found in sulfur-sufficient seeds. In the cultured seed S-adenosylmethionine (AdoMet), but not S-methylmethionine, showed a sustained rise; in the attached seed the changes were slight. The composition of the free amino acid pool did not change substantially in either recovery situation. In the cultured seed the large rise in AdoMet level occurred equally in nonrecovering seeds. It was accompanied by 6-fold and 10-fold increases in {gamma}-aminobutyrate and alanine, respectively. These effects are attributed to wounding resulting from excision of the seed. 35S-labeling experiments showed that there was no significant accumulation of label in unidentified sulfur-containing amino compounds in either recovery situation. It was concluded from these results and those of other workers that, at the present level of knowledge, the most probable candidate for a `signal' compound, eliciting recovery of legumin mRNA level in response to sulfur-feeding, is cysteine.




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F. James, K. D. Nolte, and A. D. Hanson
Purification and Properties of S-Adenosyl-L-methionine:L-Methionine S-Methyltransferase from Wollastonia biflora Leaves
J. Biol. Chem., September 22, 1995; 270(38): 22344 - 22350.
[Abstract] [Full Text] [PDF]


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Copyright © 1987 by the American Society of Plant Biologists