Abstract
Treatment of cultured parsley (Petroselinum crispum) cells with fungal elicitor rapidly activates transcription of many genes encoding specific steps in pathogen defense-related pathways. We report evidence that three cDNAs corresponding to such genes represent two key enzymes of the activated methyl cycle. Two cDNAs are derived from distinct members of the S-adenosyl-L-methionine synthetase gene family, based on extensive similarity of the deduced polypeptides with authentic enzymes from Arabidopsis thaliana, rat, yeast, and Escherichia coli. The third cDNA exhibits large similarity with a functionally related gene, encoding S-adenosyl-L-homocysteine hydrolase, from rat and a slime mold. Marked differences in the mRNA levels occurred in different organs of parsley plants. Elicitor treatment strongly induced both mRNAs in cultured cells as well as intact leaves and led to marked increases in S-adenosyl-L-homocysteine hydrolase enzyme activity. These results suggest a close metabolic link between pathogen defense and an increased turnover of activated methyl groups.
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- Adams D. O., Yang S. F. Methionine metabolism in apple tissue: implication of s-adenosylmethionine as an intermediate in the conversion of methionine to ethylene. Plant Physiol. 1977 Dec;60(6):892–896. doi: 10.1104/pp.60.6.892. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ayers A. R., Ebel J., Finelli F., Berger N., Albersheim P. Host-Pathogen Interactions: IX. Quantitative Assays of Elicitor Activity and Characterization of the Elicitor Present in the Extracellular Medium of Cultures of Phytophthora megasperma var. sojae. Plant Physiol. 1976 May;57(5):751–759. doi: 10.1104/pp.57.5.751. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen E. Y., Seeburg P. H. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA. 1985 Apr;4(2):165–170. doi: 10.1089/dna.1985.4.165. [DOI] [PubMed] [Google Scholar]
- Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Døskeland S. O., Ueland P. M. Comparison of some physicochemical and kinetic properties of S-adenosylhomocysteine hydrolase from bovine liver, bovine adrenal cortex and mouse liver. Biochim Biophys Acta. 1982 Nov 9;708(2):185–193. doi: 10.1016/0167-4838(82)90219-9. [DOI] [PubMed] [Google Scholar]
- Feinberg A. P., Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. doi: 10.1016/0003-2697(84)90381-6. [DOI] [PubMed] [Google Scholar]
- Fujioka M., Takata Y. S-Adenosylhomocysteine hydrolase from rat liver. Purification and some properties. J Biol Chem. 1981 Feb 25;256(4):1631–1635. [PubMed] [Google Scholar]
- Gomi T., Date T., Ogawa H., Fujioka M., Aksamit R. R., Backlund P. S., Jr, Cantoni G. L. Expression of rat liver S-adenosylhomocysteinase cDNA in Escherichia coli and mutagenesis at the putative NAD binding site. J Biol Chem. 1989 Sep 25;264(27):16138–16142. [PubMed] [Google Scholar]
- Gomi T., Ogawa H., Fujioka M. S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5'-p-fluorosulfonylbenzoyladenosine. J Biol Chem. 1986 Oct 15;261(29):13422–13425. [PubMed] [Google Scholar]
- Horikawa S., Ishikawa M., Ozasa H., Tsukada K. Isolation of a cDNA encoding the rat liver S-adenosylmethionine synthetase. Eur J Biochem. 1989 Oct 1;184(3):497–501. doi: 10.1111/j.1432-1033.1989.tb15042.x. [DOI] [PubMed] [Google Scholar]
- Kasir J., Aksamit R. R., Backlund P. S., Jr, Cantoni G. L. Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum as deduced from the cDNA sequence. Biochem Biophys Res Commun. 1988 May 31;153(1):359–364. doi: 10.1016/s0006-291x(88)81231-2. [DOI] [PubMed] [Google Scholar]
- Lois R., Dietrich A., Hahlbrock K., Schulz W. A phenylalanine ammonia-lyase gene from parsley: structure, regulation and identification of elicitor and light responsive cis-acting elements. EMBO J. 1989 Jun;8(6):1641–1648. doi: 10.1002/j.1460-2075.1989.tb03554.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Markham G. D., DeParasis J., Gatmaitan J. The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli. J Biol Chem. 1984 Dec 10;259(23):14505–14507. [PubMed] [Google Scholar]
- Markham G. D., Hafner E. W., Tabor C. W., Tabor H. S-Adenosylmethionine synthetase from Escherichia coli. J Biol Chem. 1980 Oct 10;255(19):9082–9092. [PubMed] [Google Scholar]
- McCue K. F., Conn E. E. Induction of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase activity by fungal elicitor in cultures of Petroselinum crispum. Proc Natl Acad Sci U S A. 1989 Oct;86(19):7374–7377. doi: 10.1073/pnas.86.19.7374. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Needleman S. B., Wunsch C. D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. doi: 10.1016/0022-2836(70)90057-4. [DOI] [PubMed] [Google Scholar]
- Ogawa H., Gomi T., Mueckler M. M., Fujioka M., Backlund P. S., Jr, Aksamit R. R., Unson C. G., Cantoni G. L. Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence. Proc Natl Acad Sci U S A. 1987 Feb;84(3):719–723. doi: 10.1073/pnas.84.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palmer J. L., Abeles R. H. The mechanism of action of S-adenosylhomocysteinase. J Biol Chem. 1979 Feb 25;254(4):1217–1226. [PubMed] [Google Scholar]
- Peleman J., Boerjan W., Engler G., Seurinck J., Botterman J., Alliotte T., Van Montagu M., Inzé D. Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase. Plant Cell. 1989 Jan;1(1):81–93. doi: 10.1105/tpc.1.1.81. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Poulton J. E., Butt V. S. Purification and properties of S-adenosyl-L-homocysteine hydrolase from leaves of spinach beet. Arch Biochem Biophys. 1976 Jan;172(1):135–142. doi: 10.1016/0003-9861(76)90058-8. [DOI] [PubMed] [Google Scholar]
- Ragg H., Kuhn D. N., Hahlbrock K. Coordinated regulation of 4-coumarate:CoA ligase and phenylalanine ammonia-lyase mRNAs in cultured plant cells. J Biol Chem. 1981 Oct 10;256(19):10061–10065. [PubMed] [Google Scholar]
- Richards H. H., Chiang P. K., Cantoni G. L. Adenosylhomocysteine hydrolase. Crystallization of the purified enzyme and its properties. J Biol Chem. 1978 Jun 25;253(12):4476–4480. [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schmelzer E., Kruger-Lebus S., Hahlbrock K. Temporal and Spatial Patterns of Gene Expression around Sites of Attempted Fungal Infection in Parsley Leaves. Plant Cell. 1989 Oct;1(10):993–1001. doi: 10.1105/tpc.1.10.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suma Y., Shimizu K., Tsukada K. Isozymes of S-adenosylmethionine synthetase from rat liver: isolation and characterization. J Biochem. 1986 Jul;100(1):67–75. doi: 10.1093/oxfordjournals.jbchem.a121707. [DOI] [PubMed] [Google Scholar]
- Tabor C. W., Tabor H. Methionine adenosyltransferase (S-adenosylmethionine synthetase) and S-adenosylmethionine decarboxylase. Adv Enzymol Relat Areas Mol Biol. 1984;56:251–282. doi: 10.1002/9780470123027.ch4. [DOI] [PubMed] [Google Scholar]
- Thomas D., Surdin-Kerjan Y. SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression. J Biol Chem. 1987 Dec 5;262(34):16704–16709. [PubMed] [Google Scholar]
- Wierenga R. K., Hol W. G. Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant. Nature. 1983 Apr 28;302(5911):842–844. doi: 10.1038/302842a0. [DOI] [PubMed] [Google Scholar]