ArticleThe Biochemical journal2005
Arabidopsis thaliana beta1,2-xylosyltransferase: an unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 62 citations in OpenAlex.
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- Hexosamine biosynthesis and related pathways, protein N-glycosylation and O-GlcNAcylation: their interconnection and role in plants.Frontiers in plant science · 2024Review
- N-glycosylation, a leading role in viral infection and immunity development.Molecular biology reports · 2022Review
- Transport, functions, and interaction of calcium and manganese in plant organellar compartments.Plant physiology · 2021Review
- Sweet Modifications Modulate Plant Development.Biomolecules · 2021Review
- ComplexFrontiers in plant science · 2021Article
- Loss of Inositol Phosphorylceramide Sphingolipid Mannosylation Induces Plant Immune Responses and Reduces Cellulose Content in Arabidopsis.The Plant cell · 2016Article
- Virulence Factors as Targets for Anticryptococcal Therapy.Journal of fungi (Basel, Switzerland) · 2016Review
- Plant protein glycosylation.Glycobiology · 2016Review
- Drosophila melanogaster cellular repressor of E1A-stimulated genes is a lysosomal protein essential for fly development.Biochimica et biophysica acta · 2014Article
- Deciphering the glycogenome of schistosomes.Frontiers in genetics · 2014Review
- Cell wall O-glycoproteins and N-glycoproteins: aspects of biosynthesis and function.Frontiers in plant science · 2014Review
- Characterizing the link between glycosylation state and enzymatic activity of the endo-β1,4-glucanase KORRIGAN1 from Arabidopsis thaliana.The Journal of biological chemistry · 2013Article
- N-glycosylation and N-glycan moieties of CTB expressed in rice seeds.Molecular biotechnology · 2013Article
- Glycosyl transferases in family 61 mediate arabinofuranosyl transfer onto xylan in grasses.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Gene sets for utilization of primary and secondary nutrition supplies in the distal gut of endangered Iberian lynx.PloS one · 2012Article
- Reduced immunogenicity of Arabidopsis hgl1 mutant N-glycans caused by altered accessibility of xylose and core fucose epitopes.The Journal of biological chemistry · 2011Article
- Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants.Molecular plant · 2011Review
- Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
XylT (beta1,2-xylosyltransferase) is a unique Golgi-bound glycosyltransferase that is involved in the biosynthesis of glycoprotein-bound N-glycans in plants. To delineate the catalytic domain of XylT, a series of N-terminal deletion mutants was heterologously expressed in insect cells. Whereas the first 54 residues could be deleted without affecting the catalytic activity of the enzyme, removal of an additional five amino acids led to the formation of an inactive protein. Characterization of the N-glycosylation status of recombinant XylT revealed that all three potential N-glycosylation sites of the protein are occupied by N-linked oligosaccharides. However, an unglycosylated version of the enzyme displayed substantial catalytic activity, demonstrating that N-glycosylation is not essential for proper folding of XylT. In contrast with most other glycosyltransferases, XylT is enzymatically active in the absence of added metal ions. This feature is not due to any metal ion directly associated with the enzyme. The precise acceptor substrate specificity of XylT was assessed with several physiologically relevant compounds and the xylosylated reaction products were subsequently tested as substrates of other Golgi-resident glycosyltransferases. These experiments revealed that the substrate specificity of XylT permits the enzyme to act at multiple stages of the plant N-glycosylation pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.