Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1993 Jun;102(2):425–433. doi: 10.1104/pp.102.2.425

Studies of the role of the propeptides of the Arabidopsis thaliana 2S albumin.

K D'Hondt 1, J Van Damme 1, C Van Den Bossche 1, S Leejeerajumnean 1, R De Rycke 1, J Derksen 1, J Vandekerckhove 1, E Krebbers 1
PMCID: PMC158796  PMID: 8108508

Abstract

To investigate the possible roles of the Arabidopsis thaliana 2S albumin propeptides with respect to sorting, processing, and stability of the protein in plant cells, five gene constructions deleting or modifying the propeptides were made based on one of the genes encoding the Arabidopsis 2S albumin. These constructions were introduced into tobacco (Nicotiana tabacum) plants. Using subcellular fractionation and immunocytochemistry on ripe seeds, it was demonstrated that none of the propeptides was necessary for the sorting of the protein. Detailed protein-chemical analysis of the mature gene products indicated that, for all of the modified 2S albumin precursors made, the proteins were stably folded and correctly processed. However, the latter is less efficient when the internal fragment between the small and the large subunit is missing or when this internal fragment is changed. In an attempt to establish a rapid assay system for modified 2S albumin precursors, yeast cells were transformed with the same gene constructs. It was demonstrated that the processing machinery in yeast cells differs from that in plants, and, in a perhaps related observation, differences in stability of a particular modified protein were observed.

Full Text

The Full Text of this article is available as a PDF (3.7 MB).

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. Bednarek S. Y., Raikhel N. V. The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell. 1991 Nov;3(11):1195–1206. doi: 10.1105/tpc.3.11.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bednarek S. Y., Wilkins T. A., Dombrowski J. E., Raikhel N. V. A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell. 1990 Dec;2(12):1145–1155. doi: 10.1105/tpc.2.12.1145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chrispeels M. J., Higgins T. J., Spencer D. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J Cell Biol. 1982 May;93(2):306–313. doi: 10.1083/jcb.93.2.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ericson M. L., Rödin J., Lenman M., Glimelius K., Josefsson L. G., Rask L. Structure of the rapeseed 1.7 S storage protein, napin, and its precursor. J Biol Chem. 1986 Nov 5;261(31):14576–14581. [PubMed] [Google Scholar]
  6. Gayler K. R., Wachsmann F., Kolivas S., Nott R., Johnson E. D. Isolation and Characterization of Protein Bodies in Lupinus angustifolius. Plant Physiol. 1989 Dec;91(4):1425–1431. doi: 10.1104/pp.91.4.1425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Guarente L., Yocum R. R., Gifford P. A GAL10-CYC1 hybrid yeast promoter identifies the GAL4 regulatory region as an upstream site. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7410–7414. doi: 10.1073/pnas.79.23.7410. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Guerche P., Tire C., De Sa F. G., De Clercq A., Van Montagu M., Krebbers E. Differential Expression of the Arabidopsis 2S Albumin Genes and the Effect of Increasing Gene Family Size. Plant Cell. 1990 May;2(5):469–478. doi: 10.1105/tpc.2.5.469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hara-Nishimura I., Inoue K., Nishimura M. A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett. 1991 Dec 2;294(1-2):89–93. doi: 10.1016/0014-5793(91)81349-d. [DOI] [PubMed] [Google Scholar]
  10. Higgins T. J., Chandler P. M., Zurawski G., Button S. C., Spencer D. The biosynthesis and primary structure of pea seed lectin. J Biol Chem. 1983 Aug 10;258(15):9544–9549. [PubMed] [Google Scholar]
  11. Holwerda B. C., Padgett H. S., Rogers J. C. Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell. 1992 Mar;4(3):307–318. doi: 10.1105/tpc.4.3.307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Klebe R. J., Harriss J. V., Sharp Z. D., Douglas M. G. A general method for polyethylene-glycol-induced genetic transformation of bacteria and yeast. Gene. 1983 Nov;25(2-3):333–341. doi: 10.1016/0378-1119(83)90238-x. [DOI] [PubMed] [Google Scholar]
  13. Krebbers E., Herdies L., De Clercq A., Seurinck J., Leemans J., Van Damme J., Segura M., Gheysen G., Van Montagu M., Vandekerckhove J. Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family. Plant Physiol. 1988 Aug;87(4):859–866. doi: 10.1104/pp.87.4.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lönnerdal B., Janson J. C. Studies on Brassica seed proteins. I. The low molecular weight proteins in rapeseed. Isolation and characterization. Biochim Biophys Acta. 1972 Aug 31;278(1):175–183. [PubMed] [Google Scholar]
  16. Matsuoka K., Nakamura K. Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):834–838. doi: 10.1073/pnas.88.3.834. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Stinissen H. M., Peumans W. J., Chrispeels M. J. Posttranslational processing of proteins in vacuoles and protein bodies is inhibited by monensin. Plant Physiol. 1985 Feb;77(2):495–498. doi: 10.1104/pp.77.2.495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Van Der Wilden W., Chrispeels M. J. Characterization of the Isozymes of alpha-Mannosidase Located in the Cell Wall, Protein Bodies, and Endoplasmic Reticulum of Phaseolus vulgaris Cotyledons. Plant Physiol. 1983 Jan;71(1):82–87. doi: 10.1104/pp.71.1.82. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. van der Klei H., Van Damme J., Casteels P., Krebbers E. A fifth 2S albumin isoform is present in Arabidopsis thaliana. Plant Physiol. 1993 Apr;101(4):1415–1416. doi: 10.1104/pp.101.4.1415. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES