Abstract
The activities of the de-N-glycosylation enzymes endo-N-acetyl- [beta]-D-glucosaminidase (ENGase; EC 3.2.1.96) and peptide-N4- (N-acetyl-[beta]-D-glucosaminyl) asparagine amidase (PNGase; EC 3.5.1.52) were monitored during germination and postgerminative development in radish (Raphanus sativus L. cv Flamboyant). The ENGase activity was detected only during postgermination, whereas the PNGase activity was present at high levels in both stages. When germination was inhibited with abscisic acid or cycloheximide, PNGase activity was detected at a basic level and ENGase activity was not detected at all. PNGase is present as an active protein in dry seeds and is apparently synthesized during seed formation. Conversely, the absence of ENGase in dry seeds suggests that its activity is dependent on the protein synthesis that occurs during and after germination. Treatment with gibberellic acid confirmed the production of both de-N-glycosylation enzymes after germination, and demonstrated a temporal delay between the production of the two enzymes during this period. Our results suggest that the two de-N-glycosylation enzymes are differentially regulated during plant development.
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- Berger S., Menudier A., Julien R., Karamanos Y. Do de-N-glycosylation enzymes have an important role in plant cells? Biochimie. 1995;77(9):751–760. doi: 10.1016/0300-9084(96)88193-4. [DOI] [PubMed] [Google Scholar]
- Berger S., Menudier A., Julien R., Karamanos Y. Endo-N-acetyl-beta-D-glucosaminidase and peptide-N4-(N-acetyl-glucosaminyl) asparagine amidase activities during germination of Raphanus sativus. Phytochemistry. 1995 Jun;39(3):481–487. doi: 10.1016/0031-9422(95)00001-n. [DOI] [PubMed] [Google Scholar]
- Bourgerie S., Berger S., Strecker G., Julien R., Karamanos Y. A fluorescence high-performance liquid chromatography assay for enzymes acting on the di-N-acetylchitobiosyl part of asparagine-linked glycans. J Biochem Biophys Methods. 1994 Jun;28(4):283–293. doi: 10.1016/0165-022x(94)90004-3. [DOI] [PubMed] [Google Scholar]
- Bourgerie S., Karamanos Y., Berger S., Julien R. Use of resorufin-labelled N-glycopeptide in a high-performance liquid chromatography assay to monitor endoglycosidase activities during cultivation of Flavobacterium meningosepticum. Glycoconj J. 1992 Aug;9(4):162–167. doi: 10.1007/BF00731160. [DOI] [PubMed] [Google Scholar]
- Chrispeels M. J., Hartl P. M., Sturm A., Faye L. Characterization of the endoplasmic reticulum-associated precursor of concanavalin A. Partial amino acid sequence and lectin activity. J Biol Chem. 1986 Aug 5;261(22):10021–10024. [PubMed] [Google Scholar]
- Lhernould S., Karamanos Y., Priem B., Morvan H. Carbon starvation increases endoglycosidase activities and production of "unconjugated N-glycans" in Silene alba cell-suspension cultures. Plant Physiol. 1994 Oct;106(2):779–784. doi: 10.1104/pp.106.2.779. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Priem B., Gross K. C. Mannosyl- and Xylosyl-Containing Glycans Promote Tomato (Lycopersicon esculentum Mill.) Fruit Ripening. Plant Physiol. 1992 Jan;98(1):399–401. doi: 10.1104/pp.98.1.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Priem B., Morvan H., Gross K. C. Unconjugated N-glycans as a new class of plant oligosaccharins. Biochem Soc Trans. 1994 May;22(2):398–402. doi: 10.1042/bst0220398. [DOI] [PubMed] [Google Scholar]
- Sheldon P. S., Bowles D. J. The glycoprotein precursor of concanavalin A is converted to an active lectin by deglycosylation. EMBO J. 1992 Apr;11(4):1297–1301. doi: 10.1002/j.1460-2075.1992.tb05173.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tretter V., Altmann F., März L. Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F cannot release glycans with fucose attached alpha 1----3 to the asparagine-linked N-acetylglucosamine residue. Eur J Biochem. 1991 Aug 1;199(3):647–652. doi: 10.1111/j.1432-1033.1991.tb16166.x. [DOI] [PubMed] [Google Scholar]
- Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology. 1993 Apr;3(2):97–130. doi: 10.1093/glycob/3.2.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
