Display options
Cite
Chrispeels MJ. The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta. 1983;158(2):140-51doi: 10.1007/BF00397707.
Chrispeels, M. J. (1983). The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta, 158(2), 140-51. https://doi.org/10.1007/BF00397707
Chrispeels, M J. "The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons." Planta vol. 158,2 (1983): 140-51. doi: https://doi.org/10.1007/BF00397707
Chrispeels MJ. The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta. 1983 Jun;158(2):140-51. doi: 10.1007/BF00397707. PMID: 24264543.
Copy Download .nbib Format: NLM
Share it on

Planta. 1983 Jun;158(2):140-51. doi: 10.1007/BF00397707.

The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons.

Planta

M J Chrispeels

Affiliations

  1. Department of Biology, C-016, University of California-San Diego, 92093, La Jolla, CA, USA.

PMID: 24264543 DOI: 10.1007/BF00397707

Abstract

When developing cotyledons of Phaseolus vulgaris L. were labeled with [(3)H]fucose, fucose-labeled phytohemagglutinin (PHA) was found in organelles with average densities of 1.13 g cm(-3) and 1.22 g cm(-3). The position of these organelles on isopycnic sucrose gradients was independent of the presence of MgCl2 and ethylenediaminetetraacetate in the media, indicating that the fucose-labeled PHA was not associated with the rough endoplasmic reticulum (ER). The organelles with a density of 1.13 g cm(-3) were identified as membranes of the Golgi apparatus on the basis of the similarity of their sedimentation properties and those of the Golgi marker enzyme, inosine diphosphatase, in both isopycnic and rate-zonal sucrose gradients. The organelles with a density of 1.22 g cm(-3) were identified as small (0.1-0.4 μm), electron-dense vesicles with a protein content similar to that of the protein bodies. Pulsechase experiments with [(3)H]fucose indicated that fucose-labeled PHA first appeared in the Golgi-apparatus-derived membranes and later in the dense vesicles. Fucose-labeled PHA chased out of the Golgi apparatus first, then out of the dense vesicles, and accumulated in the soluble portion of the homogenate which contained the contents of the broken protein bodies. Fucose-labeled PHA chased out of the two types of organelles with a t 1/2 of 20-30 min, a rate three to four times faster than newly synthesized PHA chases out of the bulk of the ER (Chrispeels, M.J., Bollini, R., 1982, Plant Physiol. 70, 1425-1428). This result indicates that the Golgi apparatus is a much smaller compartment than the ER in the storage parenchyma cells. The sodium ionophore, monensin, which interferes with the function of the Golgi apparatus of animal cells, blocks the biosynthesis and-or transport of fucose- and galactose-labeled macromolecules to the cotyledon cell walls. Monensin also blocks the transport of labeled PHA out of the Golgi apparatus and into the protein bodies. These results provide the first biochemical evidence that a specific storage protein which accumulates in seeds is modified in, and passes through, the Golgi apparatus on its way to the protein bodies.

References

  1. Plant Physiol. 1980 Sep;66(3):510-5 - PubMed
  2. Plant Physiol. 1977 Nov;60(5):703-8 - PubMed
  3. Plant Physiol. 1975 Mar;55(3):536-41 - PubMed
  4. Arch Biochem Biophys. 1975 Jul;169(1):269-77 - PubMed
  5. Eur J Biochem. 1974 Jul 1;46(1):83-8 - PubMed
  6. Planta. 1980 Dec;150(5):419-25 - PubMed
  7. Proc Natl Acad Sci U S A. 1969 Oct;64(2):605-12 - PubMed
  8. J Cell Biol. 1967 Feb;32(2):415-38 - PubMed
  9. Plant Physiol. 1978 Jan;61(1):25-9 - PubMed
  10. Biochem J. 1980 Dec 15;192(3):813-20 - PubMed
  11. Biochim Biophys Acta. 1975 Sep 9;405(1):72-81 - PubMed
  12. Planta. 1983 Apr;157(5):454-61 - PubMed
  13. Planta. 1978 Jan;142(3):291-8 - PubMed
  14. Anal Biochem. 1975 Nov;69(1):261-7 - PubMed
  15. J Biol Chem. 1982 Oct 10;257(19):11712-6 - PubMed
  16. J Cell Biol. 1983 Apr;96(4):999-1007 - PubMed
  17. Biochem J. 1980 Oct 1;191(1):257-60 - PubMed
  18. Biochim Biophys Acta. 1980 May 22;629(3):431-44 - PubMed
  19. Annu Rev Biochem. 1981;50:555-83 - PubMed
  20. Planta. 1979 Sep;146(4):487-501 - PubMed
  21. J Cell Biol. 1973 Jun;57(3):659-67 - PubMed
  22. J Biol Chem. 1975 Dec 25;250(24):9283-93 - PubMed
  23. J Cell Sci. 1969 Mar;4(2):455-97 - PubMed
  24. Plant Physiol. 1982 Nov;70(5):1425-8 - PubMed
  25. Plant Physiol. 1980 Sep;66(3):390-4 - PubMed
  26. Planta. 1979 Jan;146(1):63-9 - PubMed
  27. Plant Physiol. 1981 Aug;68(2):284-91 - PubMed
  28. J Cell Biol. 1982 Apr;93(1):5-14 - PubMed
  29. Plant Physiol. 1978 Jun;61(6):918-23 - PubMed
  30. J Biol Chem. 1980 Sep 25;255(18):8638-44 - PubMed
  31. Planta. 1970 Jun;95(2):103-18 - PubMed
  32. Plant Physiol. 1981 Feb;67(2):205-11 - PubMed
  33. J Cell Biol. 1978 Dec;79(3):694-707 - PubMed
  34. J Ultrastruct Res. 1969 Jan;26(1):31-43 - PubMed
  35. Plant Physiol. 1982 Jun;69(6):1414-7 - PubMed
  36. Planta. 1981 Nov;153(3):201-9 - PubMed
  37. Plant Mol Biol. 1981 Mar;1(1):19-34 - PubMed
  38. J Cell Biol. 1981 Dec;91(3 Pt 2):77s-103s - PubMed

Publication Types