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. 1980 Sep;66(3):390–394. doi: 10.1104/pp.66.3.390

The Endoplasmic Reticulum of Mung Bean Cotyledons

ROLE IN THE ACCUMULATION OF HYDROLASES IN PROTEIN BODIES DURING SEEDLING GROWTH 1

Willem Van der Wilden 1, Neil R Gilkes 1,2, Maarten J Chrispeels 1,3
PMCID: PMC440640  PMID: 16661442

Abstract

The subcellular localization of two hydrolases (ribonuclease and vicilin peptidohydrolase) which are synthesized de novo in the cotyledons of mung bean seedlings was studied. Earlier experiments had shown that both enzymes accumulate in the protein bodies in the course of seedling growth. Two methods to fractionate subcellular organelles were used to demonstrate that a significant proportion of the enzymes is organelle-associated. This proportion is highest (up to 50% for vicilin peptidohydrolase and 15% for ribonuclease) when synthesis of the enzymes has just started. Evidence obtained with isopycnic sucrose gradients indicates that both hydrolases are associated with membranes rich in NADH-cytochrome c reductase, a marker enzyme for the endoplasmic reticulum (ER). The hydrolases band with the NADH-cytochrome c reductase under conditions where the ribosomes remain attached or are detached from the ER-derived vesicles. Treatment of the ER-derived vesicles with Triton X-100 shows that vicilin peptidohydrolase and vesicle membranes can be physically separated without dissolving the membranes, indicating that the proteinase is soluble within the vesicles. These data support the conclusion that the ER is involved in the transport of ribonuclease and proteinase to the protein bodies.

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Selected References

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

  1. Ambellan E., Hollander V. P. A simplified assay for RNase activity in crude tissue extracts. Anal Biochem. 1966 Dec;17(3):474–484. doi: 10.1016/0003-2697(66)90182-5. [DOI] [PubMed] [Google Scholar]
  2. Baumgartner B., Chrispeels M. J. Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings. Eur J Biochem. 1977 Jul 15;77(2):223–233. doi: 10.1111/j.1432-1033.1977.tb11661.x. [DOI] [PubMed] [Google Scholar]
  3. Baumgartner B., Tokuyasu K. T., Chrispeels M. J. Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy. J Cell Biol. 1978 Oct;79(1):10–19. doi: 10.1083/jcb.79.1.10. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bowles D. J., Kauss H. Characterization, enzymatic and lectin properties of isolated membranes from Phaseolus aureus. Biochim Biophys Acta. 1976 Sep 7;443(3):360–374. doi: 10.1016/0005-2736(76)90456-9. [DOI] [PubMed] [Google Scholar]
  5. Chappell J., Van der Wilden W., Chrispeels M. J. The biosynthesis of ribonuclease and its accumulation in protein bodies in the cotyledons of mung bean seedlings. Dev Biol. 1980 Apr;76(1):115–125. doi: 10.1016/0012-1606(80)90366-8. [DOI] [PubMed] [Google Scholar]
  6. Chrispeels M. J., Baumgartner B., Harris N. Regulation of reserve protein metabolism in the cotyledons of mung bean seedlings. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3168–3172. doi: 10.1073/pnas.73.9.3168. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chrispeels M. J., Boulter D. Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase. Plant Physiol. 1975 Jun;55(6):1031–1037. doi: 10.1104/pp.55.6.1031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ericson M. C., Chrispeels M. J. Isolation and Characterization of Glucosamine-containing Storage Glycoproteins from the Cotyledons of Phaseolus aureus. Plant Physiol. 1973 Aug;52(2):98–104. doi: 10.1104/pp.52.2.98. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gilkes N. R., Chrispeels M. J. Endoplasmic Reticulum of Mung Bean Cotyledons: ACCUMULATION DURING SEED MATURATION AND CATABOLISM DURING SEEDLING GROWTH. Plant Physiol. 1980 Apr;65(4):600–604. doi: 10.1104/pp.65.4.600. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gilkes N. R., Herman E. M., Chrispeels M. J. Rapid degradation and limited synthesis of phospholipids in the cotyledons of mung bean seedlings. Plant Physiol. 1979 Jul;64(1):38–42. doi: 10.1104/pp.64.1.38. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hankins C. N., Shannon L. M. The physical and enzymatic properties of a phytohemagglutinin from mung beans. J Biol Chem. 1978 Nov 10;253(21):7791–7797. [PubMed] [Google Scholar]
  12. Harris N., Chrispeels M. J. Histochemical and biochemical observations on storage protein metabolism and protein body autolysis in cotyledons of germinating mung beans. Plant Physiol. 1975 Aug;56(2):292–299. doi: 10.1104/pp.56.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kreibich G., Debey P., Sabatini D. D. Selective release of content from microsomal vesicles without membrane disassembly. I. Permeability changes induced by low detergent concentrations. J Cell Biol. 1973 Aug;58(2):436–462. doi: 10.1083/jcb.58.2.436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lord J. M., Kagawa T., Moore T. S., Beevers H. Endoplasmic reticulum as the site of lecithin formation in castor bean endosperm. J Cell Biol. 1973 Jun;57(3):659–667. doi: 10.1083/jcb.57.3.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Van der Wilden W., Herman E. M., Chrispeels M. J. Protein bodies of mung bean cotyledons as autophagic organelles. Proc Natl Acad Sci U S A. 1980 Jan;77(1):428–432. doi: 10.1073/pnas.77.1.428. [DOI] [PMC free article] [PubMed] [Google Scholar]

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