Skip to main content
PMC home page
The Plant Cell logoLink to The Plant Cell
. 1990 Sep;2(9):941–950. doi: 10.1105/tpc.2.9.941

Two Closely Related Wheat Storage Proteins Follow a Markedly Different Subcellular Route in Xenopus laevis Oocytes.

R Simon 1, Y Altschuler 1, R Rubin 1, G Galili 1
PMCID: PMC159943  PMID: 12354972

Abstract

[alpha]-Gliadins and [gamma]-gliadins are two closely related wheat storage proteins that evolved from a common ancestral gene. However, synthesis of [alpha]-gliadins and [gamma]-gliadins in Xenopus laevis oocytes revealed striking differences in their subcellular routing. The major portion of [alpha]-gliadin accumulated inside the oocyte, whereas most of the [gamma]-gliadin was secreted. Disruption of the Golgi apparatus by monensin revealed that the major part of secretion of [gamma]-gliadin is Golgi mediated. The difference in the subcellular route between [alpha]-gliadin and [gamma]-gliadin may be attributed to differential transport from the endoplasmic reticulum to the Golgi apparatus, a process that is generally the rate-limiting step in protein secretion. Coinjection of the two mRNAs had no effect on their routing, indicating no interaction between them. Our results support the hypothesis that subcellular transport of gliadins in wheat endosperm occurs in two separate routes; one is Golgi mediated, and the other is not. We also show that the subcellular transport may be markedly affected by small structural variations within closely related storage proteins.

Full Text

The Full Text of this article is available as a PDF (2.6 MB).

Selected References

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

  1. Bassüner R., Huth A., Manteuffel R., Rapoport T. A. Secretion of plant storage globulin polypeptides by Xenopus laevis oocytes. Eur J Biochem. 1983 Jun 15;133(2):321–326. doi: 10.1111/j.1432-1033.1983.tb07465.x. [DOI] [PubMed] [Google Scholar]
  2. Bole D. G., Hendershot L. M., Kearney J. F. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell Biol. 1986 May;102(5):1558–1566. doi: 10.1083/jcb.102.5.1558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bulleid N. J., Freedman R. B. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature. 1988 Oct 13;335(6191):649–651. doi: 10.1038/335649a0. [DOI] [PubMed] [Google Scholar]
  4. Ceriotti A., Colman A. Binding to membrane proteins within the endoplasmic reticulum cannot explain the retention of the glucose-regulated protein GRP78 in Xenopus oocytes. EMBO J. 1988 Mar;7(3):633–638. doi: 10.1002/j.1460-2075.1988.tb02857.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Colman A., Bhamra S., Valle G. Post-translational modification of exogenous proteins in Xenopus laevis oocytes. Biochem Soc Trans. 1984 Dec;12(6):932–937. doi: 10.1042/bst0120932. [DOI] [PubMed] [Google Scholar]
  6. Colman A., Lane C. D., Craig R., Boulton A., Mohun T., Morser J. The influence of topology and glycosylation on the fate of heterologous secretory proteins made in Xenopus oocytes. Eur J Biochem. 1981 Jan;113(2):339–348. doi: 10.1111/j.1432-1033.1981.tb05072.x. [DOI] [PubMed] [Google Scholar]
  7. Colman A., Morser J. Export of proteins from oocytes of Xenopus laevis. Cell. 1979 Jul;17(3):517–526. doi: 10.1016/0092-8674(79)90260-5. [DOI] [PubMed] [Google Scholar]
  8. Hurkman W. J., Smith L. D., Richter J., Larkins B. A. Subcellular compartmentalization of maize storage proteins in Xenopus oocytes injected with zein messenger RNAs. J Cell Biol. 1981 May;89(2):292–299. doi: 10.1083/jcb.89.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Krieg P. A., Melton D. A. Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs. Nucleic Acids Res. 1984 Sep 25;12(18):7057–7070. doi: 10.1093/nar/12.18.7057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mains P. E., Sibley C. H. The requirement of light chain for the surface deposition of the heavy chain of immunoglobulin M. J Biol Chem. 1983 Apr 25;258(8):5027–5033. [PubMed] [Google Scholar]
  11. Olden K., Pratt R. M., Jaworski C., Yamada K. M. Evidence for role of glycoprotein carbohydrates in membrane transport: specific inhibition by tunicamycin. Proc Natl Acad Sci U S A. 1979 Feb;76(2):791–795. doi: 10.1073/pnas.76.2.791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pelham H. R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 1986 Sep 26;46(7):959–961. doi: 10.1016/0092-8674(86)90693-8. [DOI] [PubMed] [Google Scholar]
  13. Pfeffer S. R., Rothman J. E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu Rev Biochem. 1987;56:829–852. doi: 10.1146/annurev.bi.56.070187.004145. [DOI] [PubMed] [Google Scholar]
  14. Rafalski J. A., Scheets K., Metzler M., Peterson D. M., Hedgcoth C., Söll D. G. Developmentally regulated plant genes: the nucleotide sequence of a wheat gliadin genomic clone. EMBO J. 1984 Jun;3(6):1409–1415. doi: 10.1002/j.1460-2075.1984.tb01985.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WOYCHIK J. H., BOUNDY J. A., DIMLER R. J. Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch Biochem Biophys. 1961 Sep;94:477–482. doi: 10.1016/0003-9861(61)90075-3. [DOI] [PubMed] [Google Scholar]

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

RESOURCES