Skip to main content
The Plant Cell logoLink to The Plant Cell
. 1992 Sep;4(9):1053–1062. doi: 10.1105/tpc.4.9.1053

Specific expression of an extensin-like gene in the style of Nicotiana alata.

C G Chen 1, E C Cornish 1, A E Clarke 1
PMCID: PMC160196  PMID: 1392608

Abstract

cDNAs and corresponding genomic clones encoding a putative proline-rich protein (NaPRP3) were isolated from libraries prepared from Nicotiana alata style mRNA and genomic DNA. The predicted NaPRP3 protein is structurally similar to extensin in containing six copies of the characteristic extensin sequence Ser-Pro4, but differs in being smaller (151 residues compared with greater than 300 residues) and lacking Tyr residues. In contrast to most extensin genes, the NaPRP3 gene is not induced by mechanical wounding, and its expression is restricted to cells of the transmitting tract of the style.

Full Text

The Full Text of this article is available as a PDF (3.6 MB).

Selected References

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

  1. Corbin D. R., Sauer N., Lamb C. J. Differential regulation of a hydroxyproline-rich glycoprotein gene family in wounded and infected plants. Mol Cell Biol. 1987 Dec;7(12):4337–4344. doi: 10.1128/mcb.7.12.4337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Efstratiadis A., Posakony J. W., Maniatis T., Lawn R. M., O'Connell C., Spritz R. A., DeRiel J. K., Forget B. G., Weissman S. M., Slightom J. L. The structure and evolution of the human beta-globin gene family. Cell. 1980 Oct;21(3):653–668. doi: 10.1016/0092-8674(80)90429-8. [DOI] [PubMed] [Google Scholar]
  3. Feinberg A. P., Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. doi: 10.1016/0003-2697(84)90381-6. [DOI] [PubMed] [Google Scholar]
  4. Fry S. C. Isodityrosine, a new cross-linking amino acid from plant cell-wall glycoprotein. Biochem J. 1982 May 15;204(2):449–455. doi: 10.1042/bj2040449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gleeson P. A., Clarke A. E. Structural studies on the major component of Gladiolus style mucilage, an arabinogalactan-protein. Biochem J. 1979 Sep 1;181(3):607–621. doi: 10.1042/bj1810607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hong J. C., Nagao R. T., Key J. L. Developmentally regulated expression of soybean proline-rich cell wall protein genes. Plant Cell. 1989 Sep;1(9):937–943. doi: 10.1105/tpc.1.9.937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Keller B., Lamb C. J. Specific expression of a novel cell wall hydroxyproline-rich glycoprotein gene in lateral root initiation. Genes Dev. 1989 Oct;3(10):1639–1646. doi: 10.1101/gad.3.10.1639. [DOI] [PubMed] [Google Scholar]
  8. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  9. Lütcke H. A., Chow K. C., Mickel F. S., Moss K. A., Kern H. F., Scheele G. A. Selection of AUG initiation codons differs in plants and animals. EMBO J. 1987 Jan;6(1):43–48. doi: 10.1002/j.1460-2075.1987.tb04716.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol. 1983 Jun 25;167(2):391–409. doi: 10.1016/s0022-2836(83)80341-6. [DOI] [PubMed] [Google Scholar]
  11. Ye Z. H., Varner J. E. Tissue-Specific Expression of Cell Wall Proteins in Developing Soybean Tissues. Plant Cell. 1991 Jan;3(1):23–37. doi: 10.1105/tpc.3.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

Articles from The Plant Cell are provided here courtesy of Oxford University Press

RESOURCES