Function of N-glycosylation in plants

Nagashima, Yukihiro; Schaewen, Antje von; Koiwa, Hisashi

doi:10.1016/j.plantsci.2018.05.007

Cited by 114 publications

(98 citation statements)

References 135 publications

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“…At position 107, Pe HNL‐Np has an Ala residue, whereas that of Pe HNL‐Ny has a Thr residue (Figure S2). Therefore, Pe HNL cannot be glycosylated on the nitrogen atom of the Asn residue of the nascent polypeptide in the recognition tripeptide sequence Asn‐X‐Ser/Thr . Periodic acid Schiff (PAS) staining of purified Pe HNL‐Np confirmed that it was not a glycoprotein (Figure S1).…”

Section: Resultsmentioning

confidence: 99%

Stabilization of Hydroxynitrile Lyases from Two Variants of Passion Fruit, Passiflora edulis Sims and Passiflora edulis Forma flavicarpa, by C‐Terminal Truncation

et al. 2019

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Because the synthesis of chiral compounds generally requires a broad range of substrate specificity and stable enzymes, screening for better enzymes and/or improvement of enzyme properties through molecular approaches is necessary for sustainable industrial development. Herein, the discovery of unique hydroxynitrile lyases (HNLs) from two species of passion fruits, Passiflora edulis forma flavicarpa (yellow passion fruit, PeHNL‐Ny) and Passiflora edulis Sims (purple passion fruit, PeHNL‐Np), isolated and purified from passion fruit leaves is reported. These are the smallest HNLs (comprising 121 amino acids). Amino acid sequences of both enzymes are 99 % identical; there is a difference of one amino acid in a consensus sequence. PeHNL‐Np has an Ala residue at position 107 and is nonglycosylated at Asn105. Because it was confirmed that natural and glycosylated PeHNL‐Ny showed superior thermostability, pH stability, and organic tolerance to that of PeHNL‐Np, it has been speculated that protein engineering around the only glycosylation site, Asn105, located at the C‐terminal region of PeHNL‐Ny, might contribute to the stabilization of PeHNL. Therefore, the focus is on improved stability of the nonglycosylated PeHNL by truncating its C‐terminal region. The C‐terminal‐truncated PeHNLΔ107 was obtained by truncating 15 amino acids from the C terminus followed by expression in Escherichia coli. PeHNLΔ107 expressed in E. coli was not glycosylated, and showed improved thermostability, solvent stability, and reusability similar to that of the wild‐type glycosylated form of PeHNL expressed in Pichia pastoris. These data reveal that the lack of the high‐flexibility region at the C terminus of PeHNL might be a possible reason for improving the stability of PeHNL.

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Section: Resultsmentioning

confidence: 99%

Stabilization of Hydroxynitrile Lyases from Two Variants of Passion Fruit, Passiflora edulis Sims and Passiflora edulis Forma flavicarpa, by C‐Terminal Truncation

et al. 2019

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“…This indicated an ancestral intron gain in angiosperm STT3a. All STT3b genes had six exons each, with the exception of Mimulus guttatus (7) and A. thaliana (5). These exceptions might be due to species-specific intron gain and loss.…”

Section: Plant Stt3a and Stt3b Genes Are Different In Gene Structurementioning

confidence: 99%

Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms

et al. 2020

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STT3 is a catalytic subunit of hetero‐oligomeric oligosaccharyltransferase (OST), which is important for asparagine‐linked glycosylation. In mammals and plants, OSTs with different STT3 isoforms exhibit distinct levels of enzymatic efficiency or different responses to stressors. Although two different STT3 isoforms have been identified in both plants and animals, it remains unclear whether these isoforms result from gene duplication in an ancestral eukaryote. Furthermore, the molecular mechanisms underlying the functional divergences between the two STT3 isoforms in plant have not been well elucidated. Here, we conducted phylogenetic analysis of the major evolutionary node species and suggested that gene duplications of STT3 may have occurred independently in animals and plants. Across land plants, the exon–intron structure differed between the two STT3 isoforms, but was highly conserved for each isoform. Most angiosperm STT3a genes had 23 exons with intron phase 0, while STT3b genes had 6 exons with intron phase 2. Characteristic motifs (motif 18 and 19) of STT3s were mapped to different structure domains in the plant STT3 proteins. These two motifs overlap with regions of high nonsynonymous‐to‐synonymous substitution rates, suggesting the regions may be related to functional difference between STT3a and STT3b. In addition, promoter elements and gene expression profiles were different between the two isoforms, indicating expression pattern divergence of the two genes. Collectively, the identified differences may result in the functional divergence of plant STT3s.

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“…Recently different posttranslational modifications (PTMs) have been reported for peptide maturation and activation, including proteolytic processing, tyrosine sulfation, proline hydroxylation, and hydroxyproline glycosylation [7] in plants. While glycan epitopes of human complex Nglycans are often targets of lectins important for cell-cell communication, the role of plant N-glycans finds importance in protein folding, and other biological functions including salt stress responses, cellulose biosynthesis, microtubule association, and biogenesis of several receptor-like kinases [8].…”

Section: N-glycosylation In Plantsmentioning

confidence: 99%

Sialoglycans and genetically engineered plants

Ghosh¹

2020

Sialic Acids and Sialoglycoconjugates in the Biology of Life, Health and Disease

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Function of N-glycosylation in plants

Cited by 114 publications

References 135 publications

Stabilization of Hydroxynitrile Lyases from Two Variants of Passion Fruit, Passiflora edulis Sims and Passiflora edulis Forma flavicarpa, by C‐Terminal Truncation

Stabilization of Hydroxynitrile Lyases from Two Variants of Passion Fruit, Passiflora edulis Sims and Passiflora edulis Forma flavicarpa, by C‐Terminal Truncation

Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms

Sialoglycans and genetically engineered plants

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