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. 1968 May;43(5):735–742. doi: 10.1104/pp.43.5.735

Indoleacetic Acid and the Synthesis of Glucanases and Pectic Enzymes

Anne Harmon Datko 1, G A Maclachlan 1
PMCID: PMC1086918  PMID: 16656834

Abstract

Indoleacetic acid (IAA) and/or inhibitors of DNA, RNA or protein synthesis were added to the apex of decapitated seedlings of Pisum sativum L. var. Alaska. At various times up to 4 days, enzymic protein was extracted from a segment of epicotyl immediately below the apex and assayed for its ability to hydrolyse polysaccharides or their derivatives. With the exception of amylase, the total amounts per segment of all of the tested enzymes increased due to IAA treatment. The development of β-1,4-glucanase (cellulase) activity per unit of protein or fresh weight proceeded according to a typical sigmoid induction curve. Pectinase was formed for about 2 days in control segments and IAA treatment resulted in continued synthesis for at least another 2 days provided cell division took place. β-1,3-glucanase and pectinesterase activities were only enhanced by IAA to the extent that total protein levels increased. Reaction mechanisms for these effects and functions for the enzymes during growth are 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. ALBERSHEIM P., KILLIAS U. Studies relating to the purification and properties of pectin transeliminase. Arch Biochem Biophys. 1962 Apr;97:107–115. doi: 10.1016/0003-9861(62)90050-4. [DOI] [PubMed] [Google Scholar]
  2. Chrispeels M. J., Varner J. E. Gibberellic Acid-enhanced synthesis and release of alpha-amylase and ribonuclease by isolated barley and aleurone layers. Plant Physiol. 1967 Mar;42(3):398–406. doi: 10.1104/pp.42.3.398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fan D. F., Maclachlan G. A. Massive synthesis of ribonucleic Acid and cellulase in the pea epicotyl in response to indoleacetic Acid, with and without concurrent cell division. Plant Physiol. 1967 Aug;42(8):1114–1122. doi: 10.1104/pp.42.8.1114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Felicetti L., Colombo B., Baglioni C. Inhibition of protein synthesis in reticulocytes by antibiotics. II. The site of action of cycloheximide, streptovitacin A and pactamycin. Biochim Biophys Acta. 1966 Apr 18;119(1):120–129. [PubMed] [Google Scholar]
  5. Jansen E. F., Jang R. Pectic Metabolism of Growing Cell Walls. Plant Physiol. 1960 Jan;35(1):87–97. doi: 10.1104/pp.35.1.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Katz M., Ordin L. A cell wall polysaccharide-hydrolyzing enzyme system in Avena sativa L. coleoptiles. Biochim Biophys Acta. 1967 Jun 13;141(1):126–134. doi: 10.1016/0304-4165(67)90251-6. [DOI] [PubMed] [Google Scholar]
  7. Lee S. H., Kivilaan A., Bandurski R. S. In vitro autolysis of plant cell walls. Plant Physiol. 1967 Jul;42(7):968–972. doi: 10.1104/pp.42.7.968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. MARGERIE C., PEAUD-LENOEL C. [Kinetics of cellulose biosynthesis in wheat roots]. Biochim Biophys Acta. 1961 Feb 18;47:275–287. doi: 10.1016/0006-3002(61)90288-8. [DOI] [PubMed] [Google Scholar]
  9. Ray P. M. Sugar composition of oat-coleoptile cell walls. Biochem J. 1963 Oct;89(1):144–150. doi: 10.1042/bj0890144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. SHUSTER L., GIFFORD R. H. Changes in 3'-nucleotidase during the germination of wheatembryos. Arch Biochem Biophys. 1962 Mar;96:534–540. doi: 10.1016/0003-9861(62)90332-6. [DOI] [PubMed] [Google Scholar]
  11. Shannon J. C., Hanson J. B., Wilson C. M. Ribonuclease Levels in the Mesocotyl Tissue of Zea mays as a Function of 2,4-Dichlorophenoxyacetic Acid Application. Plant Physiol. 1964 Sep;39(5):804–809. doi: 10.1104/pp.39.5.804. [DOI] [PMC free article] [PubMed] [Google Scholar]

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