Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1997 Jan;113(1):65–74. doi: 10.1104/pp.113.1.65

Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood.

X H Zhang 1, V L Chiang 1
PMCID: PMC158116  PMID: 9008388

Abstract

Two genomic sequences encoding 4-coumarate:coenzyme A ligase (4CL; EC 6.2.1.12) in loblolly pine (Pinus taeda L.) were cloned. Both sequences contained three introns and four exons with identical coding sequences predicting 537 amino acids. Two of the three introns in these two clones were different both in sequence and in length. Sequences of both 4CL clones were found in all nine megagametophyte DNAs tested, providing genetic evidence that these two 4CL genomic sequences are nonallelic genes. Our analyses suggest that there are at least two distinct, intron-containing 4CL genes, at least one of which is transcribed into 4CL mRNA in developing xylem tissue of loblolly pine. The levels of 4CL gene transcription in xylem were influenced by compressional stress, resulting in an elevated 4CL enzyme activity with 4-coumaric acid. 4CL enzyme activity with ferulic acid remained unchanged, whereas with caffeic acid it was significantly inhibited. Exogenously applied trans-cinnamic acid in the protein extracts from normal wood xylem caused inhibition of 4CL activity toward caffeic acid similar to that under compressional stress. The implications of this cinnamic acid-modulated effect on 4CL enzyme activities toward different substrates in regulating monolignol synthesis in xylem under compressional stress are discussed.

Full Text

The Full Text of this article is available as a PDF (2.5 MB).

Selected References

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

  1. Becker-André M., Schulze-Lefert P., Hahlbrock K. Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate: CoA ligase genes in potato. J Biol Chem. 1991 May 5;266(13):8551–8559. [PubMed] [Google Scholar]
  2. Bugos R. C., Chiang V. L., Zhang X. H., Campbell E. R., Podila G. K., Campbell W. H. RNA isolation from plant tissues recalcitrant to extraction in guanidine. Biotechniques. 1995 Nov;19(5):734–737. [PubMed] [Google Scholar]
  3. Douglas C., Hoffmann H., Schulz W., Hahlbrock K. Structure and elicitor or u.v.-light-stimulated expression of two 4-coumarate:CoA ligase genes in parsley. EMBO J. 1987 May;6(5):1189–1195. doi: 10.1002/j.1460-2075.1987.tb02353.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Goodall G. J., Filipowicz W. The AU-rich sequences present in the introns of plant nuclear pre-mRNAs are required for splicing. Cell. 1989 Aug 11;58(3):473–483. doi: 10.1016/0092-8674(89)90428-5. [DOI] [PubMed] [Google Scholar]
  5. Gross G. G., Zenk M. H. Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia. Eur J Biochem. 1974 Mar 1;42(2):453–459. doi: 10.1111/j.1432-1033.1974.tb03359.x. [DOI] [PubMed] [Google Scholar]
  6. Knobloch K. H., Hahlbrock K. 4-Coumarate:CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Partial purification, substrate specificity, and further properties. Arch Biochem Biophys. 1977 Nov;184(1):237–248. doi: 10.1016/0003-9861(77)90347-2. [DOI] [PubMed] [Google Scholar]
  7. Knobloch K. H., Hahlbrock K. Isoenzymes of p-coumarate: CoA ligase from cell suspension cultures of Glycine max. Eur J Biochem. 1975 Mar 17;52(2):311–320. doi: 10.1111/j.1432-1033.1975.tb03999.x. [DOI] [PubMed] [Google Scholar]
  8. Lamb C. J. Regulation of enzyme levels in phenylpropanoid biosynthesis: characterization of the modulation by light and pathway intermediates. Arch Biochem Biophys. 1979 Jan;192(1):311–317. doi: 10.1016/0003-9861(79)90097-3. [DOI] [PubMed] [Google Scholar]
  9. Lange B. M., Lapierre C., Sandermann H., Jr Elicitor-Induced Spruce Stress Lignin (Structural Similarity to Early Developmental Lignins). Plant Physiol. 1995 Jul;108(3):1277–1287. doi: 10.1104/pp.108.3.1277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lee D., Douglas C. J. Two divergent members of a tobacco 4-coumarate:coenzyme A ligase (4CL) gene family. cDNA structure, gene inheritance and expression, and properties of recombinant proteins. Plant Physiol. 1996 Sep;112(1):193–205. doi: 10.1104/pp.112.1.193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lee D., Ellard M., Wanner L. A., Davis K. R., Douglas C. J. The Arabidopsis thaliana 4-coumarate:CoA ligase (4CL) gene: stress and developmentally regulated expression and nucleotide sequence of its cDNA. Plant Mol Biol. 1995 Aug;28(5):871–884. doi: 10.1007/BF00042072. [DOI] [PubMed] [Google Scholar]
  12. Loake G. J., Choudhary A. D., Harrison M. J., Mavandad M., Lamb C. J., Dixon R. A. Phenylpropanoid pathway intermediates regulate transient expression of a chalcone synthase gene promoter. Plant Cell. 1991 Aug;3(8):829–840. doi: 10.1105/tpc.3.8.829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Loake G. J., Faktor O., Lamb C. J., Dixon R. A. Combination of H-box [CCTACC(N)7CT] and G-box (CACGTG) cis elements is necessary for feed-forward stimulation of a chalcone synthase promoter by the phenylpropanoid-pathway intermediate p-coumaric acid. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9230–9234. doi: 10.1073/pnas.89.19.9230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., Hahlbrock K. Primary structures and catalytic properties of isoenzymes encoded by the two 4-coumarate: CoA ligase genes in parsley. Eur J Biochem. 1988 Oct 1;176(3):661–667. doi: 10.1111/j.1432-1033.1988.tb14328.x. [DOI] [PubMed] [Google Scholar]
  15. Lüderitz T., Schatz G., Grisebach H. Enzymic synthesis of lignin precursors. Purification and properties of 4-coumarate:CoA ligase from cambial sap of spruce (Picea abies L.). Eur J Biochem. 1982 Apr;123(3):583–586. [PubMed] [Google Scholar]
  16. Mavandad M., Edwards R., Liang X., Lamb C. J., Dixon R. A. Effects of trans-Cinnamic Acid on Expression of the Bean Phenylalanine Ammonia-Lyase Gene Family. Plant Physiol. 1990 Oct;94(2):671–680. doi: 10.1104/pp.94.2.671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Orr J. D., Edwards R., Dixon R. A. Stress Responses in Alfalfa (Medicago sativa L.) (XIV. Changes in the Levels of Phenylpropanoid Pathway Intermediates in Relation to Regulation of L-Phenylalanine Ammonia-Lyase in Elicitor-Treated Cell-Suspension Cultures). Plant Physiol. 1993 Mar;101(3):847–856. doi: 10.1104/pp.101.3.847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ranjeva R., Boudet A. M., Faggion R. Phenolic metabolism in petunia tissues. IV. - Properties of p-coumarate : coenzyme A ligase isoenzymes. Biochimie. 1976;58(10):1255–1262. doi: 10.1016/s0300-9084(76)80125-3. [DOI] [PubMed] [Google Scholar]
  19. Uhlmann A., Ebel J. Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an enzyme involved in the resistance response of soybean (Glycine max L.) against pathogen attack. Plant Physiol. 1993 Aug;102(4):1147–1156. doi: 10.1104/pp.102.4.1147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Voo K. S., Whetten R. W., O'Malley D. M., Sederoff R. R. 4-coumarate:coenzyme a ligase from loblolly pine xylem. Isolation, characterization, and complementary DNA cloning. Plant Physiol. 1995 May;108(1):85–97. doi: 10.1104/pp.108.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zhao Y., Kung S. D., Dube S. K. Nucleotide sequence of rice 4-coumarate:CoA ligase gene, 4-CL.1. Nucleic Acids Res. 1990 Oct 25;18(20):6144–6144. doi: 10.1093/nar/18.20.6144. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES