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. 1989 Nov;91(3):911–916. doi: 10.1104/pp.91.3.911

Increase of Chalcone Synthase mRNA in Pathogen-Inoculated Soybeans with Race-Specific Resistance Is Different in Leaves and Roots 1

Shree Dhawale 1,2, Ginette Souciet 1,3, David N Kuhn 1
PMCID: PMC1062095  PMID: 16667156

Abstract

Soybeans (Glycine max [L.] Merr.) respond to pathogens by producing isoflavonoid-derived phytoalexins. Chalcone synthase (CHS) is the first enzyme of the flavonoid/isoflavonoid biosynthetic pathway. We investigated changes in the steady state levels of CHS mRNA and other specific mRNAs at increasing times after inoculation in two different race-specific interactions, one between leaves and the bacterium Pseudomonas syringae pv glycinea (Psg), and one between roots and the fungus, Phytophthora megasperma f. sp. glycinea (Pmg). The amount of CHS mRNA increases significantly in soybean leaves inoculated with an avirulent race of Psg but not with a virulent race or water. In contrast, the increase in CHS mRNA is similar in roots inoculated with zoospores of either an avirulent or virulent race of Pmg. CHS mRNA increases significantly in pathogen inoculated roots but not in uninoculated controls. Hydroxyproline-rich glycoprotein (HRGP) has been observed by others to increase in wounded or pathogen-inoculated plants. We report here that HRGP mRNA levels are greater in roots inoculated with an avirulent Pmg race than with a virulent race, but inoculation with either race causes a significant increase in HRGP mRNA with respect to controls. Calmodulin or ubiquitin mRNA do not increase in either uninoculated or inoculated roots and leaves. The possibility that race-specific resistance in soybeans is expressed differently in different organs of the plant is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chen J., Varner J. E. Isolation and characterization of cDNA clones for carrot extensin and a proline-rich 33-kDa protein. Proc Natl Acad Sci U S A. 1985 Jul;82(13):4399–4403. doi: 10.1073/pnas.82.13.4399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dixon R. A., Dey P. M., Lamb C. J. Phytoalexins: enzymology and molecular biology. Adv Enzymol Relat Areas Mol Biol. 1983;55:1–136. doi: 10.1002/9780470123010.ch1. [DOI] [PubMed] [Google Scholar]
  3. Ebel J., Schmidt W. E., Loyal R. Phytoalexin synthesis in soybean cells: elicitor induction of phenylalanine ammonia-lyase and chalcone synthase mRNAs and correlation with phytoalexin accumulation. Arch Biochem Biophys. 1984 Jul;232(1):240–248. doi: 10.1016/0003-9861(84)90540-x. [DOI] [PubMed] [Google Scholar]
  4. Hahn M. G., Bonhoff A., Grisebach H. Quantitative Localization of the Phytoalexin Glyceollin I in Relation to Fungal Hyphae in Soybean Roots Infected with Phytophthora megasperma f. sp. glycinea. Plant Physiol. 1985 Mar;77(3):591–601. doi: 10.1104/pp.77.3.591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kosslak R. M., Bookland R., Barkei J., Paaren H. E., Appelbaum E. R. Induction of Bradyrhizobium japonicum common nod genes by isoflavones isolated from Glycine max. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7428–7432. doi: 10.1073/pnas.84.21.7428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Lagacé L., Chandra T., Woo S. L., Means A. R. Identification of multiple species of calmodulin messenger RNA using a full length complementary DNA. J Biol Chem. 1983 Feb 10;258(3):1684–1688. [PubMed] [Google Scholar]
  7. Napoli C., Staskawicz B. Molecular characterization and nucleic acid sequence of an avirulence gene from race 6 of Pseudomonas syringae pv. glycinea. J Bacteriol. 1987 Feb;169(2):572–578. doi: 10.1128/jb.169.2.572-578.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Parish J. H., Kirby K. S. Reagents which reduce interactions between ribosomal RNA and rapidly labelled RNA from rat liver. Biochim Biophys Acta. 1966 Dec 21;129(3):554–562. doi: 10.1016/0005-2787(66)90070-0. [DOI] [PubMed] [Google Scholar]
  9. Peters N. K., Frost J. W., Long S. R. A plant flavone, luteolin, induces expression of Rhizobium meliloti nodulation genes. Science. 1986 Aug 29;233(4767):977–980. doi: 10.1126/science.3738520. [DOI] [PubMed] [Google Scholar]
  10. Rave N., Crkvenjakov R., Boedtker H. Identification of procollagen mRNAs transferred to diazobenzyloxymethyl paper from formaldehyde agarose gels. Nucleic Acids Res. 1979 Aug 10;6(11):3559–3567. doi: 10.1093/nar/6.11.3559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ryder T. B., Cramer C. L., Bell J. N., Robbins M. P., Dixon R. A., Lamb C. J. Elicitor rapidly induces chalcone synthase mRNA in Phaseolus vulgaris cells at the onset of the phytoalexin defense response. Proc Natl Acad Sci U S A. 1984 Sep;81(18):5724–5728. doi: 10.1073/pnas.81.18.5724. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ryder T. B., Hedrick S. A., Bell J. N., Liang X. W., Clouse S. D., Lamb C. J. Organization and differential activation of a gene family encoding the plant defense enzyme chalcone synthase in Phaseolus vulgaris. Mol Gen Genet. 1987 Dec;210(2):219–233. doi: 10.1007/BF00325687. [DOI] [PubMed] [Google Scholar]
  13. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wiborg O., Pedersen M. S., Wind A., Berglund L. E., Marcker K. A., Vuust J. The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. EMBO J. 1985 Mar;4(3):755–759. doi: 10.1002/j.1460-2075.1985.tb03693.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

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