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. 1993 Nov;103(3):719–726. doi: 10.1104/pp.103.3.719

Expression and Localization of Plant Protein Disulfide Isomerase.

B S Shorrosh 1, J Subramaniam 1, K R Schubert 1, R A Dixon 1
PMCID: PMC159041  PMID: 12231974

Abstract

A cDNA clone encoding a putative protein disulfide isomerase (PDI, EC 5.3.4.1) from alfalfa (Medicago sativa L.) was expressed in Escherichia coli cells, and an antiserum was raised against the expressed PDI-active protein. The antiserum recognized a protein of approximately 60 kD in extracts from alfalfa, soybean, and tobacco roots and stems. Levels of this protein remained relatively constant on exposure of alfalfa cell suspension cultures to the protein glycosylation inhibitor tunicamycin, whereas a slightly lower molecular mass form, also detected by the antiserum, was induced by this treatment. A lower molecular mass form of PDI was also observed in roots of alfalfa seedlings during the first 5 weeks after germination. PDI levels increased in developing soybean seeds up to 17 d after fertilization and then declined. Tissue print immunoblots revealed highest levels of PDI protein in the cambial tissues of soybean stems and petioles and in epidermal, subepidermal, cortical, and pith tissues of stems of alfalfa and tobacco. Immunogold electron microscopy confirmed the localization of PDI to the endoplasmic reticulum in soybean root nodules.

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Selected References

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  1. Bolwell G. P., Robbins M. P., Dixon R. A. Metabolic changes in elicitor-treated bean cells. Enzymic responses associated with rapid changes in cell wall components. Eur J Biochem. 1985 May 2;148(3):571–578. doi: 10.1111/j.1432-1033.1985.tb08878.x. [DOI] [PubMed] [Google Scholar]
  2. 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]
  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. Cheng S. Y., Gong Q. H., Parkison C., Robinson E. A., Appella E., Merlino G. T., Pastan I. The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J Biol Chem. 1987 Aug 15;262(23):11221–11227. [PubMed] [Google Scholar]
  5. Edman J. C., Ellis L., Blacher R. W., Roth R. A., Rutter W. J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature. 1985 Sep 19;317(6034):267–270. doi: 10.1038/317267a0. [DOI] [PubMed] [Google Scholar]
  6. Geetha-Habib M., Noiva R., Kaplan H. A., Lennarz W. J. Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER. Cell. 1988 Sep 23;54(7):1053–1060. doi: 10.1016/0092-8674(88)90120-1. [DOI] [PubMed] [Google Scholar]
  7. Noiva R., Kimura H., Roos J., Lennarz W. J. Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen. J Biol Chem. 1991 Oct 15;266(29):19645–19649. [PubMed] [Google Scholar]
  8. Noiva R., Lennarz W. J. Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem. 1992 Feb 25;267(6):3553–3556. [PubMed] [Google Scholar]
  9. Robertson E. F., Dannelly H. K., Malloy P. J., Reeves H. C. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal Biochem. 1987 Dec;167(2):290–294. doi: 10.1016/0003-2697(87)90166-7. [DOI] [PubMed] [Google Scholar]
  10. Shorrosh B. S., Dixon R. A. Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase. Plant J. 1992 Jan;2(1):51–58. doi: 10.1046/j.1365-313x.1992.t01-50-00999.x. [DOI] [PubMed] [Google Scholar]
  11. Shorrosh B. S., Dixon R. A. Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10941–10945. doi: 10.1073/pnas.88.23.10941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Walling L., Drews G. N., Goldberg R. B. Transcriptional and post-transcriptional regulation of soybean seed protein mRNA levels. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2123–2127. doi: 10.1073/pnas.83.7.2123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wetterau J. R., Combs K. A., McLean L. R., Spinner S. N., Aggerbeck L. P. Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein. Biochemistry. 1991 Oct 8;30(40):9728–9735. doi: 10.1021/bi00104a023. [DOI] [PubMed] [Google Scholar]
  14. Wetterau J. R., Combs K. A., Spinner S. N., Joiner B. J. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem. 1990 Jun 15;265(17):9800–9807. [PubMed] [Google Scholar]
  15. Ye Z. H., Varner J. E. Tissue-Specific Expression of Cell Wall Proteins in Developing Soybean Tissues. Plant Cell. 1991 Jan;3(1):23–37. doi: 10.1105/tpc.3.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Yoshimori T., Semba T., Takemoto H., Akagi S., Yamamoto A., Tashiro Y. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem. 1990 Sep 15;265(26):15984–15990. [PubMed] [Google Scholar]

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