Skip to main content
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1969 Jan 1;53(1):1–20. doi: 10.1085/jgp.53.1.1

Timing of the Auxin Response in Coleoptiles and Its Implications Regarding Auxin Action

Michael L Evans 1, Peter M Ray 1
PMCID: PMC2202898  PMID: 5761870

Abstract

The timing of the auxin response was followed in oat and corn coleoptile tissue by a sensitive optical method in which the elongation of about a dozen coleoptile segments was recorded automatically. The response possesses a latent period of about 10 min at 23°C, which is extended by low concentrations of KCN or by reducing the temperature, but is not extended by pretreatments with actinomycin D, puromycin, or cycloheximide at concentrations that partially inhibit the elongation response. Analysis of the data indicates that auxin probably does not act on the elongation of these tissues by promoting the synthesis of informational RNA or of enzymatic protein. Not excluded is the possibility that auxin acts at the translational level to induce synthesis of a structural protein, such as cell wall protein or membrane protein. While the data do not provide direct support for this hypothesis, the speed with which cycloheximide inhibits elongation suggests that continual protein synthesis may be important in the mechanism of cell wall expansion.

Full Text

The Full Text of this article is available as a PDF (1.2 MB).

Selected References

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

  1. Alpers D. H., Tomkins G. M. Sequential transcription of the genes of the lactose operon and its regulation by protein synthesis. J Biol Chem. 1966 Oct 10;241(19):4434–4443. [PubMed] [Google Scholar]
  2. BOROUGHS H., BONNER J. Effects of indoleacetic acid on metabolic pathways. Arch Biochem Biophys. 1953 Oct;46(2):279–290. doi: 10.1016/0003-9861(53)90201-x. [DOI] [PubMed] [Google Scholar]
  3. Baker R. F., Yanofsky C. The periodicity of RNA polymerase initiations: a new regulatory feature of transcription. Proc Natl Acad Sci U S A. 1968 May;60(1):313–320. doi: 10.1073/pnas.60.1.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chroboczek H., Cherry J. H. Characterization of nucleic acids in peanut cotyledons. J Mol Biol. 1966 Aug;19(1):28–37. doi: 10.1016/s0022-2836(66)80047-5. [DOI] [PubMed] [Google Scholar]
  5. Cleland R. Inhibition of formation of protein-bound hydroxyproline by free hydroxyproline in Avena coleoptiles. Plant Physiol. 1967 Sep;42(9):1165–1170. doi: 10.1104/pp.42.9.1165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Coartney J. S., Morre D. J., Key J. L. Inhibition of RNA synthesis and auxin-induced cell wall extensibility and growth by Actinomycin D. Plant Physiol. 1967 Mar;42(3):434–439. doi: 10.1104/pp.42.3.434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cove D. J. Kinetic studies of the induction of nitrate reductase and cytochrome c reductase in the fungus Aspergillus nidulans. Biochem J. 1967 Sep;104(3):1033–1039. doi: 10.1042/bj1041033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cozzone A., Marchis-Mouren G. Messenger ribonucleic acid stability in rat pancreas and liver. Biochemistry. 1967 Dec;6(12):3911–3917. doi: 10.1021/bi00864a037. [DOI] [PubMed] [Google Scholar]
  9. DINTZIS H. M. Assembly of the peptide chains of hemoglobin. Proc Natl Acad Sci U S A. 1961 Mar 15;47:247–261. doi: 10.1073/pnas.47.3.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fristrom J. W., Brothers L., Mancebo V., Stewart D. Aspects of RNA and protein synthesis in imaginal discs of Drosophila melanogaster. Mol Gen Genet. 1968;102(1):1–14. doi: 10.1007/BF00341865. [DOI] [PubMed] [Google Scholar]
  11. Garren L. D., Ney R. L., Davis W. W. Studies on the role of protein synthesis in the regulation of corticosterone production by adrenocorticotropic hormone in vivo. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1443–1450. doi: 10.1073/pnas.53.6.1443. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Glasziou K. T., Waldron J. C., Bull T. A. Control of invertase synthesis in sugar cane. Loci of auxin and glucose effects. Plant Physiol. 1966 Feb;41(2):282–288. doi: 10.1104/pp.41.2.282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. INGLE J., KEY J. L., HOLM R. E. DEMONSTRATION AND CHARACTERIZATION OF A DNA-LIKE RNA IN EXCISED PLANT TISSUE. J Mol Biol. 1965 Apr;11:730–746. doi: 10.1016/s0022-2836(65)80031-6. [DOI] [PubMed] [Google Scholar]
  14. Korner A. Ribonucleic acid and hormonal control of protein synthesis. Prog Biophys Mol Biol. 1967;17:61–98. doi: 10.1016/0079-6107(67)90004-1. [DOI] [PubMed] [Google Scholar]
  15. Leive L., Kollin V. Synthesis, utilization and degradation of lactose operon mRNA in Escherichia coli. J Mol Biol. 1967 Mar 14;24(2):247–259. doi: 10.1016/0022-2836(67)90330-0. [DOI] [PubMed] [Google Scholar]
  16. Lin C. Y., Key J. L. Dissocation and reassembly of polyribosomes in relation to protein synthesis in the soybean root. J Mol Biol. 1967 Jun 14;26(2):237–247. doi: 10.1016/0022-2836(67)90294-x. [DOI] [PubMed] [Google Scholar]
  17. Nooden L. D. Studies on the role of RNA synthesis in auxin induction of cell enlargement. Plant Physiol. 1968 Feb;43(2):140–150. doi: 10.1104/pp.43.2.140. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pickett-Heaps J. D. Further observations on the Golgi apparatus and its functions in cells of the wheat seedling. J Ultrastruct Res. 1967 May;18(3):287–303. doi: 10.1016/s0022-5320(67)80119-9. [DOI] [PubMed] [Google Scholar]
  19. Ray P. M. Radioautographic study of cell wall deposition in growing plant cells. J Cell Biol. 1967 Dec;35(3):659–674. doi: 10.1083/jcb.35.3.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SOKOLOFF L., FRANCIS C. M., CAMPBELL P. L. THYROXINE STIMULATION OF AMINO ACID INCORPORATION INTO PROTEIN INDEPENDENT OF ANY ACTION ON MESSENGER RNA SYNTHESIS. Proc Natl Acad Sci U S A. 1964 Sep;52:728–736. doi: 10.1073/pnas.52.3.728. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Shearer R. W., McCarthy B. J. Evidence for ribonucleic acid molecules restricted to the cell nucleus. Biochemistry. 1967 Jan;6(1):283–289. doi: 10.1021/bi00853a044. [DOI] [PubMed] [Google Scholar]
  22. Singer M. F., Leder P. Messenger RNA: an evaluation. Annu Rev Biochem. 1966;35:195–230. doi: 10.1146/annurev.bi.35.070166.001211. [DOI] [PubMed] [Google Scholar]
  23. Tuli V., Moyed H. S. Inhibitory oxidation products of indole-3-acetic Acid: 3-hydroxymethyloxindole and 3-methyleneoxindole as plant metabolites. Plant Physiol. 1967 Mar;42(3):425–430. doi: 10.1104/pp.42.3.425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zimmermann R. A., Levinthal C. Messenger RNA and RNA transcription time. J Mol Biol. 1967 Dec 14;30(2):349–370. [PubMed] [Google Scholar]

Articles from The Journal of General Physiology are provided here courtesy of The Rockefeller University Press

RESOURCES