Do de-N-glycosylation enzymes have an important role in plant cells?

Berger, Sylvie; Menudier, Aline; Julien, Raymond; Karamanos, Yannis

doi:10.1016/0300-9084(96)88193-4

Cited by 27 publications

(27 citation statements)

References 88 publications

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“…All these arguments appear to concur that PNGase has yet undefined physiological role in plant and animal cells and to confirm our previous proposal that the N-glycosylation/de-Nglycosylation system should occur more commonly than presently recognized in living organisms (28,38,39). Possible involvement of PNGase in the processes that initiate and control the metabolic activities of plant and animal development by free oligosaccharides liberated from glycoproteins has been substantiated by their accumulation, although the underlying molecular mechanisms are in most cases unknown.…”

supporting

confidence: 67%

“…(d) In addition to possible function of generating free glycans, PNGase-catalyzed de-N-glycosylation of plant glycoproteins was proposed as a possible mechanism for regulating protein activity by removing N-glycans and converting glycosylated Asn residues to the Asp residues (9,28,38,39). A specific PNGase seems to have a specific function during early embryogenesis (e.g.…”

Section: Discussionmentioning

confidence: 99%

“…[25][26][27][28][29][30]. Unconjugated N-glycans (29) were isolated from the extracellular medium of a plant-cell suspension of white campion, Silene alba (25,26) as well as from the tomato fruit pericarp (Ref.…”

mentioning

confidence: 99%

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Developmentally Regulated Expression of a Peptide:N-Glycanase during Germination of Rice Seeds (Oryza sativa) and Its Purification and Characterization

Chang

Kuo

Khoo

et al. 2000

Journal of Biological Chemistry

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Peptide:N-glycanase (PNGase; EC 3.5.1.52) activity was detected in dormant rice seeds (Oryza sativa) and the imbibed rice grains. Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm-and embryo tissue-containing areas, and started to increase only in growing germ part, reached a peak at about 3-day stage, followed by a gradual decrease concomitant with a sharp increase in the coleoptile. The specific activity increased about 6-fold at about 3-day stage. PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h, and the apparent molecular weight of the purified enzyme, estimated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), was about 80,000. The purified enzyme was designated PNGase Os to denote its origin. The N-terminal sequence of the 10 residues was determined to be SYN-VASVAGL. The purified PNGase Os in SDS-PAGE appeared as a rather broad band, consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column. PNGase expressed in coleoptile under anoxia condition was also purified, and both of the purified enzymes were found to exhibit very similar, if not identical, electrophoretic mobility in SDS-PAGE. PNGase Os exhibited a broad pH-activity profile with an optimum of 4 -5 and, interestingly, was significantly inactivated by K ؉ and Na ؉ at near the physiological concentration, 100 mM. These results are discussed in relation to other work.-(N-acetyl-␤-Dglucosaminyl) asparagine amidase, EC 3.5.1.52) had only been known to occur in some plant seeds (1-5) and bacteria (6) and used as a useful reagent in a number of studies of structure and function of glycoproteins having N-linked glycan chains until we demonstrated for the first time its occurrence in the early embryos of Medaka fish, Oryzias latipes in 1991 (7). Following this discovery, we began to focus our interest on the physiological significance of this enzyme in living organisms because little attention had been paid to it. In view of the unique structural change in a given functional protein by converting the glycosylated asparagine residue to the aspartic acid residue upon de-N-glycosylation catalyzed by PNGase as the posttranslational remodification of protein, we anticipated that N-glycosylation of proteins by oligosaccharyltransferase and their de-N-glycosylation by PNGase constitute a basic biological mechanism of functioning within cells (8, 9). For understanding the biological meaning of the occurrence of PNGase in eukaryotes, we have been involved in a series of studies on animal-derived PNGases (10 -15) and reported the following. (a) PNGase activities were shown to occur in mammalianderived cell lines including human origin (10). (b) PNGase activities were detected ubiquitously in various organs and tissues of mouse (13). (c) PNGase was purified to homogeneity from the confluent stage of C3H mouse fibroblast L-929 cells and characterized to serve not only a...

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supporting

confidence: 67%

Section: Discussionmentioning

confidence: 99%

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Developmentally Regulated Expression of a Peptide:N-Glycanase during Germination of Rice Seeds (Oryza sativa) and Its Purification and Characterization

Chang

Kuo

Khoo

et al. 2000

Journal of Biological Chemistry

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“…However, there is strong evidence that these enzymes catalyze the hydrolytic decomposition of arabinogalactan proteins (AGPs) present in plants (van Hengel et al 2001(van Hengel et al , 2002. Other N-acetylglucosamine-containing glycoproteins present in the cell wall may be endogenous substrates for plant chitinases (Berger et al 1995;Schultze et al 1998;van der Holst et al 2001;Dyachok et al 2002). It has also been suggested that exochitinases have probable roles in the degradation of reserve glycoproteins during seed germination (Poulton et al 1985) and N-glycan metabolism during ripening in apple fruit (Choi and Gross 1994).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays

Shoresh

Harman

2008

Mol Genet Genomics

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Chitinolytic enzymes are important pathogenesis and stress related proteins. We identiWed 27 putative genes encoding endochitinases in the maize genome via in silico techniques and four exochitinases. Only seven of the endochitinases and segments of the exochitinases were heretofore known. The endochitinases included members of family 19 chitinases (classes I-IV of PR3, II of PR4) and members of family 18 chitinases (class III of PR8). Some similar enzymes were detected on adjacent regions of the same chromosome, and seem to result from duplication events. Most of the genes expressed were identiWed from EST libraries from plants exposed to biotic or abiotic stresses but also from libraries from tissues not exposed to stresses. We isolated proteins from seedlings of maize in the presence or absence of the symbiotic root colonizing fungus Trichoderma harzianum strain T22, and analyzed the activity of chitinolytic enzymes using an in-gel activity assay. The activity bands were identiWed by LC/MS/MS using the database from our in silico study. The identities of the enzymes changed depending on whether or not T22 was present. One activity band of about 95 kDa appeared to be a heterodimer between an exochitinase and any of several diVerent endochitinases. The identity of the endochitinase component appeared to be dependent upon treatment.

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“…A few biological roles were suggested for the plant enzymes (reviewed in [9]). PNGase J can contribute to the process of activation of the lectin Concanavalin A (Con A) produced by Canavalia ensiformis and found in significant Amidases: More than Just Tools amounts in seeds.…”

Section: Occurrence Characteristics and Functions Of Pngasesmentioning

confidence: 99%

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

Karamanos¹

2013

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Abstract:Since the discovery of endo-N-acetyl-β-D-glucosaminidases (ENGase) and peptide-N4-(N-acetyl-β-D-glucosaminyl) asparagine amidases (PNGase) most of the published work described their use for structural studies. Less attention was given to the potential roles of those enzymes in the physiology of the cells/organisms they produced them. The scope of this review is firstly to analyse the data on the occurrence and characteristics of murein-, chitin-, and N-glycan-ENGases acting on GlcNAc-containing polymers in three structural families, namely murein, chitin, and N-glycosylproteins, and of PNGases, only acting on N-glycosylproteins, and secondly to discuss the biological roles of the enzymes in the producing cells. The analysis demonstrates the remarkable diversity of the enzymes, and simultaneously the interest of studying their substrate specificity and their structural features. Many examples illustrate the importance of the structure/function relationships studies. Diverse biological roles were anticipated, e.g. they are useful for feeding purposes, are implicated in pathogenesis processes, modulate the activity of macromolecules, and help in the destruction of misfolded proteins. Their effect can be direct or indirect, through the reaction products. Current knowledge only partially explains the biological roles of ENGases and PNGases, thus further studies are expected for determining novel possibilities and elucidating other cell pathways.

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Do de-N-glycosylation enzymes have an important role in plant cells?

Cited by 27 publications

References 88 publications

Developmentally Regulated Expression of a Peptide:N-Glycanase during Germination of Rice Seeds (Oryza sativa) and Its Purification and Characterization

Developmentally Regulated Expression of a Peptide:N-Glycanase during Germination of Rice Seeds (Oryza sativa) and Its Purification and Characterization

Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

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