ArticlePlant physiology2017
Soluble and Membrane-Bound β-Glucosidases Are Involved in Trimming the Xyloglucan Backbone.
Article in Plant physiology, 2017. 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, 39 citations in OpenAlex.
- Ipecac alkaloid biosynthesis in two evolutionarily distant plants.Nature chemical biology · 2025Article
- Characterization and Expression Analysis of β-Glucosidase Gene Under Abiotic Stresses in Pepper (Genes · 2025Article
- Modulation of morphogenesis and metabolism by plant cell biomechanics: from model plants to traditional herbs.Horticulture research · 2025Article
- Genome-wide identification and gene expression pattern analysis of the glycoside hydrolase family 1 in Fagopyrum tataricum.BMC plant biology · 2024Article
- Global impacts of peroxisome and pexophagy dysfunction revealed through multi-omics analyses of lon2 and atg2 mutants.The Plant journal : for cell and molecular biology · 2024Article
- Whole-Genome Sequencing and Analysis of Tumour-Forming Radish (International journal of molecular sciences · 2024Article
- Whole-genome sequencing and comparative genomics reveal candidate genes associated with quality traits in Dioscorea alata.BMC genomics · 2024Article
- Xyloglucan remodelling enzymes and the mechanics of plant seed and fruit biology.Journal of experimental botany · 2022Article
- Forgotten Actors: Glycoside Hydrolases During Elongation Growth of Maize Primary Root.Frontiers in plant science · 2021Article
- Phylogenomics of Plant-AssociatedFrontiers in microbiology · 2021Article
- Genome-Wide Association Studies Identifying Multiple Loci Associated With Alfalfa Forage Quality.Frontiers in plant science · 2021Article
- A Group of O-Acetyltransferases Catalyze Xyloglucan Backbone Acetylation and Can Alter Xyloglucan Xylosylation Pattern and Plant Growth When Expressed in Arabidopsis.Plant & cell physiology · 2020Article
- Xyloglucan exoglycosidases in the monocot model Brachypodium distachyon and the conservation of xyloglucan disassembly in angiosperms.Plant molecular biology · 2019Article
- Sugar metabolism as input signals and fuel for leaf senescence.Genes & genomics · 2019Review
- Glycosylphosphatidylinositol-Anchored Proteins inFrontiers in plant science · 2019Review
- Analysis of Xyloglucan Composition inBio-protocol · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In many flowering plants, xyloglucan is a major component of primary cell walls, where it plays an important role in growth regulation. Xyloglucan can be degraded by a suite of exoglycosidases that remove specific sugars. In this work, we show that the xyloglucan backbone, formed by (1→4)-linked β-d-glucopyranosyl residues, can be attacked by two different Arabidopsis (Arabidopsis thaliana) β-glucosidases from glycoside hydrolase family 3. While BGLC1 (At5g20950; for β-glucosidase active against xyloglucan 1) is responsible for all or most of the soluble activity, BGLC3 (At5g04885) is usually a membrane-anchored protein. Mutations in these two genes, whether on their own or combined with mutations in other exoglycosidase genes, resulted in the accumulation of partially digested xyloglucan subunits, such as GXXG, GXLG, or GXFG. While a mutation in BGLC1 had significant effects on its own, lack of BGLC3 had only minor effects. On the other hand, double bglc1 bglc3 mutants revealed a synergistic interaction that supports a role for membrane-bound BGLC3 in xyloglucan metabolism. In addition, bglc1 bglc3 was complemented by overexpression of either BGLC1 or BGLC3 In overexpression lines, BGLC3 activity was concentrated in a microsome-enriched fraction but also was present in soluble form. Finally, both genes were generally expressed in the same cell types, although, in some cases, BGLC3 was expressed at earlier stages than BGLC1 We propose that functional specialization could explain the separate localization of both enzymes, as a membrane-bound β-glucosidase could specifically digest soluble xyloglucan without affecting the wall-bound polymer.
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