ArticleBMC biochemistry2012
Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum.
Article in BMC biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- NGLY1 mutations cause protein aggregation in human neurons.Cell reports · 2023Article
- Reversibility of motor dysfunction in the rat model of NGLY1 deficiency.Molecular brain · 2021Article
- JF1/B6F1 Ngly1Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021Article
- Ngly1 -/- rats develop neurodegenerative phenotypes and pathological abnormalities in their peripheral and central nervous systems.Human molecular genetics · 2020Article
- Investigating the Role of Translationally Control Tumor Protein in Growth, Development and Differentiation ofFrontiers in cell and developmental biology · 2020Article
- Data on the expression and purification of Sestrin protein fromData in brief · 2019Article
- Deletion of Dictyostelium discoideum Sir2A impairs cell proliferation and inhibits autophagy.Journal of biosciences · 2018Article
- Aberrant adhesion impacts early development in a Dictyostelium model for juvenile neuronal ceroid lipofuscinosis.Cell adhesion & migration · 2017Article
- Article
- Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene.PLoS genetics · 2017Article
- Altered N-glycosylation modulates TgrB1- and TgrC1-mediated development but not allorecognition in Dictyostelium.Journal of cell science · 2015Article
- Classification and expression analyses of homeobox genes from Dictyostelium discoideum.Journal of biosciences · 2015Article
- Endo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathway.Genetics in medicine : official journal of the American College of Medical Genetics · 2014Article
- Analysis of Rheb in the cellular slime mold Dictyostelium discoideum: cellular localization, spatial expression and overexpression.Journal of biosciences · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPeptide: N- glycanase (PNGase) enzyme cleaves oligosaccharides from the misfolded glycoproteins and prepares them for degradation. This enzyme plays a role in the endoplasmic reticulum associated degradation (ERAD) pathway in yeast and mice but its biological importance and role in multicellular development remain largely unknown.
resultsIn this study, the PNGase from the cellular slime mold, Dictyostelium discoideum (DdPNGase) was identified based on the presence of a common TG (transglutaminase) core domain and its sequence homology with the known PNGases. The domain architecture and the sequence comparison validated the presence of probable functional domains in DdPNGase. The tertiary structure matched with the mouse PNGase. Here we show that DdPNGase is an essential protein, required for aggregation during multicellular development and a knockout strain of it results in small sized aggregates, all of which did not form fruiting bodies. The in situ hybridization and RT-PCR results show higher level of expression during the aggregate stage. The expression gets restricted to the prestalk region during later developmental stages. DdPNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity.
conclusionsWe have identified and characterized a novel PNGase from D. discoideum and confirmed its deglycosylation activity. The results emphasize the importance of PNGase in aggregation during multicellular development of this organism.
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