Skip to main content
NCBI home page
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1987 Dec;7(12):4273–4279. doi: 10.1128/mcb.7.12.4273

Expression of a gene encoding a glycine-rich protein in petunia.

C M Condit 1, R B Meagher 1
PMCID: PMC368109  PMID: 2449603

Abstract

We have investigated the expression of a gene that codes for a glycine-rich structural protein (GRP1) in petunia. This gene is expressed as a single polyadenylated RNA of approximately 1,600 bases which was found to be present in leaves, stems, and flowers of petunia but not in roots. In the organs in which GRP1-specific mRNA was expressed, its steady-state levels were highest in stems and leaves and lowest in flowers. This analysis also revealed that the pattern of organ-specific expression for several of the GRP1-related genes was distinctly different. In addition, it was found that the levels of GRP1 RNA were significantly higher in young leaves and stems than in old, implying developmental regulation of the gene. GRP1-specific RNA in both old and young tissue that had been wounded was found to be increased at least 25-fold over that in young unwounded tissue. Increased levels of GRP1 mRNA were seen within 5 min after wounding, with substantial increases apparent by 30 min. Maximal levels of accumulation of GRP1 transcripts occurred 90 min after wounding. The enhancement of GRP1 mRNA levels by wounding appears to be one of the earliest events of the plant wound response and is distinct from that which we observed for the PAL gene in petunia. Using S1 analysis and RNA primer extension, we demonstrated that the same transcriptional start site was used by the GRP1 gene in all organs and in wounded and unwounded tissue. The potential significance of these data with regard to wound signal transduction is discussed.

Full text

PDF
4273

Images in this article

4275Image
on p.4275
4276Image
on p.4276
4276Image
on p.4276
4277Image
on p.4277
4278Image
on p.4278

Selected References

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

  1. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bell J. N., Ryder T. B., Wingate V. P., Bailey J. A., Lamb C. J. Differential accumulation of plant defense gene transcripts in a compatible and an incompatible plant-pathogen interaction. Mol Cell Biol. 1986 May;6(5):1615–1623. doi: 10.1128/mcb.6.5.1615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berridge M. J., Irvine R. F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature. 1984 Nov 22;312(5992):315–321. doi: 10.1038/312315a0. [DOI] [PubMed] [Google Scholar]
  4. Cassab G. I., Nieto-Sotelo J., Cooper J. B., van Holst G. J., Varner J. E. A developmentally regulated hydroxyproline-rich glycoprotein from the cell walls of soybean seed coats. Plant Physiol. 1985 Mar;77(3):532–535. doi: 10.1104/pp.77.3.532. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chen J., Varner J. E. An extracellular matrix protein in plants: characterization of a genomic clone for carrot extensin. EMBO J. 1985 Sep;4(9):2145–2151. doi: 10.1002/j.1460-2075.1985.tb03908.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cooper J. B., Varner J. E. Cross-linking of soluble extensin in isolated cell walls. Plant Physiol. 1984 Oct;76(2):414–417. doi: 10.1104/pp.76.2.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eckenrode V. K., Arnold J., Meagher R. B. Comparison of the nucleotide sequence of soybean 18S rRNA with the sequences of other small-subunit rRNAs. J Mol Evol. 1984;21(3):259–269. doi: 10.1007/BF02102358. [DOI] [PubMed] [Google Scholar]
  8. Edwards K., Cramer C. L., Bolwell G. P., Dixon R. A., Schuch W., Lamb C. J. Rapid transient induction of phenylalanine ammonia-lyase mRNA in elicitor-treated bean cells. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6731–6735. doi: 10.1073/pnas.82.20.6731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Favaloro J., Treisman R., Kamen R. Transcription maps of polyoma virus-specific RNA: analysis by two-dimensional nuclease S1 gel mapping. Methods Enzymol. 1980;65(1):718–749. doi: 10.1016/s0076-6879(80)65070-8. [DOI] [PubMed] [Google Scholar]
  10. Greenberg M. E., Ziff E. B., Greene L. A. Stimulation of neuronal acetylcholine receptors induces rapid gene transcription. Science. 1986 Oct 3;234(4772):80–83. doi: 10.1126/science.3749894. [DOI] [PubMed] [Google Scholar]
  11. Lawton M. A., Lamb C. J. Transcriptional activation of plant defense genes by fungal elicitor, wounding, and infection. Mol Cell Biol. 1987 Jan;7(1):335–341. doi: 10.1128/mcb.7.1.335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Majerus P. W., Neufeld E. J., Wilson D. B. Production of phosphoinositide-derived messengers. Cell. 1984 Jul;37(3):701–703. doi: 10.1016/0092-8674(84)90405-7. [DOI] [PubMed] [Google Scholar]
  13. Mort A. J., Lamport D. T. Anhydrous hydrogen fluoride deglycosylates glycoproteins. Anal Biochem. 1977 Oct;82(2):289–309. doi: 10.1016/0003-2697(77)90165-8. [DOI] [PubMed] [Google Scholar]
  14. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  15. Saunders M. J., Hepler P. K. Calcium antagonists and calmodulin inhibitors block cytokinin-induced bud formation in Funaria. Dev Biol. 1983 Sep;99(1):41–49. doi: 10.1016/0012-1606(83)90252-x. [DOI] [PubMed] [Google Scholar]
  16. Shah D. M., Hightower R. C., Meagher R. B. Complete nucleotide sequence of a soybean actin gene. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1022–1026. doi: 10.1073/pnas.79.4.1022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Showalter A. M., Bell J. N., Cramer C. L., Bailey J. A., Varner J. E., Lamb C. J. Accumulation of hydroxyproline-rich glycoprotein mRNAs in response to fungal elicitor and infection. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6551–6555. doi: 10.1073/pnas.82.19.6551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shure M., Wessler S., Fedoroff N. Molecular identification and isolation of the Waxy locus in maize. Cell. 1983 Nov;35(1):225–233. doi: 10.1016/0092-8674(83)90225-8. [DOI] [PubMed] [Google Scholar]
  19. Thomas E. D. Bone marrow grafts and tolerance. Nature. 1986 Sep 11;323(6084):110–111. doi: 10.1038/323110b0. [DOI] [PubMed] [Google Scholar]
  20. Treisman R., Proudfoot N. J., Shander M., Maniatis T. A single-base change at a splice site in a beta 0-thalassemic gene causes abnormal RNA splicing. Cell. 1982 Jul;29(3):903–911. doi: 10.1016/0092-8674(82)90452-4. [DOI] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES