Skip to main content
PMC home page
The EMBO Journal logoLink to The EMBO Journal
. 1988 Sep;7(9):2631–2635. doi: 10.1002/j.1460-2075.1988.tb03115.x

In vivo import of plastocyanin and a fusion protein into developmentally different plastids of transgenic plants

Douwe de Boer 1,2, Fons Cremers 1, Renske Teertstra 1, Lianne Smits 1, Jacques Hille 3, Sjef Smeekens 1,2, Peter Weisbeek 1,2
PMCID: PMC457049  PMID: 15977334

Abstract

Transgenic tomato plants that constitutively express a foreign plastocyanin gene were used to study protein transport in different tissues. Normally expression of endogenous plastocyanin genes in plants is restricted to photosynthetic tissues only, whereas this foreign plastocyanin protein is found to be present in all tissues examined. The protein is transported into the local plastids in these tissues and it is processed to the mature size. We conclude that plastids of developmentally different tissues are capable of importing precursor proteins that are normally not found in these tissues. Most likely such plastids, though functionally and morphologically differentiated, have similar or identical protein import mechanisms when compared to the chloroplasts in green tissue.

Keywords: in vivo protein transport, transgenic tomato plants, non-leaf tissue

Full text

PDF
2634

Images in this article

2632Image
on p.2632
2632Image
on p.2632
2633Image
on p.2633
2633Image
on p.2633
2634Image
on p.2634

Selected References

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

  1. A simple and general method for transferring genes into plants. Science. 1985 Mar 8;227(4691):1229–1231. doi: 10.1126/science.227.4691.1229. [DOI] [PubMed] [Google Scholar]
  2. Bevan M. Binary Agrobacterium vectors for plant transformation. Nucleic Acids Res. 1984 Nov 26;12(22):8711–8721. doi: 10.1093/nar/12.22.8711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boonstra J., van Maurik P., Defize L. H., de Laat S. W., Leunissen J. L., Verkley A. J. Visualization of epidermal growth factor receptor in cryosections of cultured A431 cells by immuno-gold labeling. Eur J Cell Biol. 1985 Mar;36(2):209–216. [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  5. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  6. Cline K., Werner-Washburne M., Lubben T. H., Keegstra K. Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J Biol Chem. 1985 Mar 25;260(6):3691–3696. [PubMed] [Google Scholar]
  7. Coruzzi G., Broglie R., Edwards C., Chua N. H. Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase. EMBO J. 1984 Aug;3(8):1671–1679. doi: 10.1002/j.1460-2075.1984.tb02031.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dobberstein B., Blobel G., Chua N. H. In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5-bisphosphate carboxylase of Chlamydomonas reinhardtii. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1082–1085. doi: 10.1073/pnas.74.3.1082. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  10. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  11. Lamppa G., Nagy F., Chua N. H. Light-regulated and organ-specific expression of a wheat Cab gene in transgenic tobacco. Nature. 1985 Aug 22;316(6030):750–752. doi: 10.1038/316750a0. [DOI] [PubMed] [Google Scholar]
  12. Meinkoth J., Wahl G. Hybridization of nucleic acids immobilized on solid supports. Anal Biochem. 1984 May 1;138(2):267–284. doi: 10.1016/0003-2697(84)90808-x. [DOI] [PubMed] [Google Scholar]
  13. Odell J. T., Nagy F., Chua N. H. Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter. 1985 Feb 28-Mar 6Nature. 313(6005):810–812. doi: 10.1038/313810a0. [DOI] [PubMed] [Google Scholar]
  14. Pain D., Blobel G. Protein import into chloroplasts requires a chloroplast ATPase. Proc Natl Acad Sci U S A. 1987 May;84(10):3288–3292. doi: 10.1073/pnas.84.10.3288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pain D., Kanwar Y. S., Blobel G. Identification of a receptor for protein import into chloroplasts and its localization to envelope contact zones. Nature. 1988 Jan 21;331(6153):232–237. doi: 10.1038/331232a0. [DOI] [PubMed] [Google Scholar]
  16. Robinson C., Ellis R. J. Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in the processing of important precursor polypeptides. Eur J Biochem. 1984 Jul 16;142(2):337–342. doi: 10.1111/j.1432-1033.1984.tb08291.x. [DOI] [PubMed] [Google Scholar]
  17. Sanders P. R., Winter J. A., Barnason A. R., Rogers S. G., Fraley R. T. Comparison of cauliflower mosaic virus 35S and nopaline synthase promoters in transgenic plants. Nucleic Acids Res. 1987 Feb 25;15(4):1543–1558. doi: 10.1093/nar/15.4.1543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schindler C., Soll J. Protein transport in intact, purified pea etioplasts. Arch Biochem Biophys. 1986 May 15;247(1):211–220. doi: 10.1016/0003-9861(86)90550-3. [DOI] [PubMed] [Google Scholar]
  19. Schmidt G. W., Mishkind M. L. The transport of proteins into chloroplasts. Annu Rev Biochem. 1986;55:879–912. doi: 10.1146/annurev.bi.55.070186.004311. [DOI] [PubMed] [Google Scholar]
  20. Smeekens S., Bauerle C., Hageman J., Keegstra K., Weisbeek P. The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell. 1986 Aug 1;46(3):365–375. doi: 10.1016/0092-8674(86)90657-4. [DOI] [PubMed] [Google Scholar]
  21. Smeekens S., van Binsbergen J., Weisbeek P. The plant ferredoxin precursor: nucleotide sequence of a full length cDNA clone. Nucleic Acids Res. 1985 May 10;13(9):3179–3194. doi: 10.1093/nar/13.9.3179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The EMBO Journal are provided here courtesy of Nature Publishing Group

RESOURCES