ArticleThe Journal of biological chemistry2012
Characterization of the arabinogalactan protein 31 (AGP31) of Arabidopsis thaliana: new advances on the Hyp-O-glycosylation of the Pro-rich domain.
Article in The Journal of biological chemistry, 2012. 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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Who cites it
24 citing papers in PubMed.
- Comprehensive Genome-Wide Investigation and Transcriptional Regulation of the bZIP Gene Family in Litchi Fruit Development.Plants (Basel, Switzerland) · 2025Article
- Knockout of eightCell surface (Amsterdam, Netherlands) · 2023Article
- Arabinogalactan-Proteins as Boron-Acting Enzymes, Cross-Linking the Rhamnogalacturonan-II Domains of Pectin.Plants (Basel, Switzerland) · 2023Review
- Article
- An Arabidopsis thaliana arabinogalactan-protein (AGP31) and several cationic AGP fragments catalyse the boron bridging of rhamnogalacturonan-II.The Biochemical journal · 2022Article
- Arabinogalactan Proteins: Focus on the Role in Cellulose Synthesis and Deposition during Plant Cell Wall Biogenesis.International journal of molecular sciences · 2022Review
- New insights on the expression patterns of specific Arabinogalactan proteins in reproductive tissues ofFrontiers in plant science · 2022Article
- Somatic Embryogenesis inPlants (Basel, Switzerland) · 2020Review
- The Cell Wall PAC (Proline-Rich, Arabinogalactan Proteins, Conserved Cysteines) Domain-Proteins Are Conserved in the Green Lineage.International journal of molecular sciences · 2020Article
- On the Potential Function of Type II ArabinogalactanFrontiers in plant science · 2020Review
- Identification of Hydroxyproline-Containing Proteins and Hydroxylation of Proline Residues in Rice.Frontiers in plant science · 2020Article
- HyPRP1 performs a role in negatively regulating cotton resistance to V. dahliae via the thickening of cell walls and ROS accumulation.BMC plant biology · 2018Article
- Formation of the Stomatal Outer Cuticular Ledge Requires a Guard Cell Wall Proline-Rich Protein.Plant physiology · 2017Article
- Proline Hydroxylation in Cell Wall Proteins: Is It Yet Possible to Define Rules?Frontiers in plant science · 2017Article
- Bioinformatics Prediction and Evolution Analysis of Arabinogalactan Proteins in the Plant Kingdom.Frontiers in plant science · 2017Article
- Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis.International journal of molecular sciences · 2016Article
- Identification of the Abundant Hydroxyproline-Rich Glycoproteins in the Root Walls of Wild-Type Arabidopsis, an ext3 Mutant Line, and Its Phenotypic Revertant.Plants (Basel, Switzerland) · 2015Article
- Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques.Frontiers in plant science · 2015Article
- Arabinogalactan protein 31 (AGP31), a putative network-forming protein in Arabidopsis thaliana cell walls?Annals of botany · 2014Article
- Salt stress in Arabidopsis: lipid transfer protein AZI1 and its control by mitogen-activated protein kinase MPK3.Molecular plant · 2014Article
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6 authors.
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Abstract
Proteins are important actors in plant cell walls because they contribute to their architecture and their dynamics. Among them, hydroxyproline (Hyp)-rich glycoproteins constitute a complex family of O-glycoproteins with various structures and functions. In this study, we characterized an atypical Hyp-rich glycoprotein, AGP31 (arabinogalactan protein 31), which displays a multidomain organization unique in Arabidopsis thaliana, consisting of a short arabinogalactan protein (AGP) motif, a His stretch, a Pro-rich domain, and a C-terminal PAC (PRP-AGP containing Cys) domain. The use of various mass spectrometry strategies was innovative and powerful: it permitted us to locate Hyp residues, to demonstrate the presence of carbohydrates, and to refine their distribution over the Pro-rich domain. Most Hyp were isolated within repeated motifs such as KAOV, KSOV, K(PO/OP)T, K(PO/OP)V, T(PO/OP)V, and Y(PO/OP)T. A few extensin-like motifs with contiguous Hyp (SOOA and SOOT) were also found. The Pro-rich domain was shown to carry Gal residues on isolated Hyp but also Ara residues. The existence of new type Hyp-O-Gal/Ara-rich motifs not recognized by the β-glucosyl Yariv reagent but interacting with the peanut agglutinin lectin was proposed. In addition, the N-terminal short AGP motif was assumed to be substituted by arabinogalactans. Altogether, AGP31 was found to be highly heterogeneous in cell walls because arabinogalactans could be absent, Hyp-O-Gal/Ara-rich motifs of different sizes were observed, and truncated forms missing the C-terminal PAC domain were found, suggesting degradation in muro and/or partial glycosylation prior to secretion.
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