Structure of a plant β-galactosidase C-terminal domain

Rimlumduan, Thipwarin; Hua, Yuexuan; Tanaka, Toŝhiyuki; Cairns, James R. Ketudat

doi:10.1016/j.bbapap.2016.07.005

Cited by 4 publications

(2 citation statements)

References 40 publications

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“…This domain, if present, is a C-terminal domain that is homologous to galactose-and rhamnose-binding animal lectins, which is designated a SUEL (Sea Urchin Egg Lectin)-type carbohydrate-binding domain. The structure and function of this domain in rice β-galactosidase, OsBGal1, was studied in detail (Rimlumduan et al, 2016). Although the binding of galactose and rhamnose was predicted for OsBGal1 based on amino acid sequence homology with SUEL lectin, binding to rhamnose, galactose, glucose, β-1,4-galactobiose, and raffinose was not observed in NMR experiments.…”

Section: Differentially Expressed Flax Lectins Between Samples With Distinct Cell Wall Typesmentioning

confidence: 99%

Gene Expression Patterns for Proteins With Lectin Domains in Flax Stem Tissues Are Related to Deposition of Distinct Cell Wall Types

et al. 2021

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The genomes of higher plants encode a variety of proteins with lectin domains that are able to specifically recognize certain carbohydrates. Plants are enriched in a variety of potentially complementary glycans, many of which are located in the cell wall. We performed a genome-wide search for flax proteins with lectin domains and compared the expression of the encoding genes in different stem tissues that have distinct cell wall types with different sets of major polysaccharides. Over 400 genes encoding proteins with lectin domains that belong to different families were revealed in the flax genome; three quarters of these genes were expressed in stem tissues. Hierarchical clustering of the data for all expressed lectins grouped the analyzed samples according to their characteristic cell wall type. Most lectins differentially expressed in tissues with primary, secondary, and tertiary cell walls were predicted to localize at the plasma membrane or cell wall. These lectins were from different families and had various architectural types. Three out of four flax genes for proteins with jacalin-like domains were highly upregulated in bast fibers at the stage of tertiary cell wall deposition. The dynamic changes in transcript level of many genes for lectins from various families were detected in stem tissue over the course of gravitropic response induced by plant gravistimulation. The data obtained in this study indicate a large number of lectin-mediated events in plants and provide insight into the proteins that take part in tissue specialization and reaction to abiotic stress.

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Section: Differentially Expressed Flax Lectins Between Samples With Distinct Cell Wall Typesmentioning

confidence: 99%

Gene Expression Patterns for Proteins With Lectin Domains in Flax Stem Tissues Are Related to Deposition of Distinct Cell Wall Types

et al. 2021

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“…Eight conserved cysteine residues are also found in many extracellular binding domains and help form disulfide bonds to increase protein stability ( Chantarangsee et al 2007 ), suggesting that the BGAL C-terminal domain may support efficient binding with galactose-containing substrates such as cell wall polysaccharides and glycoproteins ( Trainotti et al 2001 ; Triantafillidou and Georgatsos 2001 ; Esteban et al 2005 ; Iglesias et al 2006 ). While this C-terminal domain has a structure similar to that of rhamnose-binding lectins, it does not bind to galactose or rhamnose when produced as an isolated domain ( Rimlumduan et al 2016 ), so its precise function remains unclear.…”

Section: Introductionmentioning

confidence: 99%

SPOTTED-LEAF7 targets the gene encoding β-galactosidase9, which functions in rice growth and stress responses

Hoang

Rahman

et al. 2023

Plant Physiology

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β-Galactosidases (Bgals) remove terminal β-D-galactosyl residues from the non-reducing ends of β-D-galactosides and oligosaccharides. Bgals are present in bacteria, fungi, animals, and plants and have various functions. Despite many studies on the evolution of BGALs in plants, their functions remain obscure. Here, we identified rice (Oryza sativa) β-galactosidase9 (OsBGAL9) as a direct target of the heat stress-induced transcription factor SPOTTED-LEAF7 (OsSPL7), as demonstrated by protoplast transactivation analysis and yeast one-hybrid and electrophoretic mobility shift assays. Knockout plants for OsBGAL9 (Osbgal9) showed short stature and growth retardation. Histochemical ß-glucuronidase (GUS) analysis of transgenic lines harboring an OsBGAL9pro:GUS reporter construct revealed that OsBGAL9 is mainly expressed in internodes at the mature stage. OsBGAL9 expression was barely detectable in seedlings under normal conditions but increased in response to biotic and abiotic stresses. Ectopic expression of OsBGAL9 enhanced resistance to the rice pathogens Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae, as well as tolerance to cold and heat stress, while Osbgal9 mutant plants showed the opposite phenotypes. OsBGAL9 localized to the cell wall, suggesting that OsBGAL9 and its plant putative orthologs likely evolved functions distinct from those of its closely related animal enzymes. Enzyme activity assays and analysis of the cell wall composition of OsBGAL9 overexpression and mutant plants indicated that OsBGAL9 has activity toward galactose residues of arabinogalactan proteins (AGPs). Our study clearly demonstrates a role for a member of the BGAL family in AGP processing during plant development and stress responses.

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Transcriptome profiling uncovers β-galactosidases of diverse domain classes influencing hypocotyl development in jute (Corchorus capsularis L.)

et al. 2018

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Structure of a plant β-galactosidase C-terminal domain

Cited by 4 publications

References 40 publications

Gene Expression Patterns for Proteins With Lectin Domains in Flax Stem Tissues Are Related to Deposition of Distinct Cell Wall Types

Gene Expression Patterns for Proteins With Lectin Domains in Flax Stem Tissues Are Related to Deposition of Distinct Cell Wall Types

SPOTTED-LEAF7 targets the gene encoding β-galactosidase9, which functions in rice growth and stress responses

Transcriptome profiling uncovers β-galactosidases of diverse domain classes influencing hypocotyl development in jute (Corchorus capsularis L.)

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