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beta glucosidase/lituruoho
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 59 tuloksia
Arabidopsis thaliana beta-Glucosidases BGLU45 and BGLU46 hydrolyse monolignol glucosides.
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In higher plants, beta-glucosidases belonging to glycoside hydrolase (GH) Family 1 have been implicated in several fundamental processes including lignification. Phylogenetic analysis of Arabidopsis thaliana GH Family 1 has revealed that At1g61810 (BGLU45), At1g61820 (BGLU46), and At4g21760 (BGLU47)
A phosphate-starvation inducible beta-glucosidase gene (psr3.2) isolated from Arabidopsis thaliana is a member of a distinct subfamily of the BGA family.
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We have previously isolated a phosphate starvation-response (psr) cDNA clone, psr3.1, from Brassica nigra which encodes a beta-glucosidase. Southern blots of Arabidopsis thaliana genomic DNA probed with the psr3.1 cDNA indicated that this gene exists as a single locus. A genomic library of A.
A pseudo-beta-glucosidase in Arabidopsis thaliana: correction by site-directed mutagenesis, heterologous expression, purification, and characterization.
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Since At2g25630 is an intronless gene with a premature stop codon, its cDNA encoding the predicted mature beta-glucosidase isoenzyme was synthesized from the previously isolated Arabidopsis thaliana genomic DNA. The stop codon was converted to a sense codon by site-directed mutagenesis. The native
Arabidopsis thaliana β-glucosidase BGLU15 attacks flavonol 3-O-β-glucoside-7-O-α-rhamnosides.
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Kaempferol and quercetin 3-O-β-glucoside-7-O-α-rhamnoside (K3G7R and Q3G7R, respectively) are major flavonol bisglycosides accumulating in Arabidopsis thaliana with synergistic abiotic stresses (i.e., nitrogen deficiency and low temperature, NDLT). However, these molecules disappear rapidly during
The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific beta-glucosidases.
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Plants develop various ER-derived structures with specific functions. The ER body found in Arabidopsis thaliana is a spindle-shaped structure. ER bodies accumulate in epidermal cells in seedlings or are induced by wounding. The molecular mechanisms underlying the formation of the ER body remained
Demonstration of monolignol β-glucosidase activity of rice Os4BGlu14, Os4BGlu16 and Os4BGlu18 in Arabidopsis thaliana bglu45 mutant.
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The glycoside hydrolase family 1 members Os4BGlu14, Os4BGlu16, and Os4BGlu18 were proposed to be rice monolignol β-glucosidases. In vitro studies demonstrated that the Os4BGlu16 and Os4BGlu18 hydrolyze the monolignol glucosides coniferin and syringin with high efficiency compared to other
N-glycosylation is involved in stomatal development partially by modulating the release of active abscisic acid and auxin by β-glucosidase in Arabidopsis thaliana
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Asparagine-linked glycosylation (N-glycosylation) is one of the most important protein modifications in eukaryotes, affecting the folding, transport, and function of a wide range of proteins. However, it is still less known about the roles of N-glycosylation in the development of stomata in plants.
PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and the endophytic fungus Piriformospora indica.
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Piriformospora indica, an endophyte of the Sebacinaceae family, promotes growth and seed production of many plant species, including Arabidopsis. Growth of a T-DNA insertion line in PYK10 is not promoted and the plants do not produce more seeds in the presence of P. indica, although their roots are
Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases.
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The endoplasmic reticulum (ER) body is an ER-related organelle that accumulates high levels of PYK10, a beta-glucosidase with an ER retention signal. Constitutive ER bodies are present in the epidermal cells of cotyledons, hypocotyls and roots of young Arabidopsis seedlings, but absent in rosette
Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana.
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PYK10/BGLU23 is a beta-glucosidase that is a major protein of ER bodies, which are endoplasmic reticulum (ER)-derived organelles that may be involved in defense systems. PYK10 has active and inactive forms. Active PYK10 molecules form large complexes with diameters ranging from 0.65 microm to > 70
Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana.
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The ER body is an endoplasmic reticulum (ER)-derived organelle. Because ER bodies are induced by wounding and methyl jasmonate (MeJA) treatment in rosette leaves, they might be responsible for defense systems. Recently, we isolated nai1 mutants that have no ER body and showed that the levels of
The SENSITIVE TO FREEZING2 gene, required for freezing tolerance in Arabidopsis thaliana, encodes a beta-glucosidase.
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The sensitive to freezing2-1 (sfr2-1) mutation causes freezing sensitivity in Arabidopsis thaliana. By mapping, transgenic complementation, and sequencing, sfr2-1 was revealed to be a mutation in gene At3g06510. A new knockout allele was obtained, and its identical freezing-sensitive phenotype
Soluble and Membrane-Bound β-Glucosidases Are Involved in Trimming the Xyloglucan Backbone.
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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
The bglX gene located at 47.8 min on the Escherichia coli chromosome encodes a periplasmic beta-glucosidase.
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A new Escherichia coli gene, bgIX, encoding a beta-D-glucosidase (EC 3.2.1.21) has been characterized. The bgIX gene is located adjacent to the dld gene at 47.8 min or 2225 kb on the E. coli chromosome. The sequence of a 2.6 kb DNA fragment from this region revealed a large open reading frame
Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana.
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All four glycanases necessary for the degradation of xyloglucan oligosaccharides (alpha-fucosidase, alpha-xylosidase, beta-galactosidase and beta-glucosidase) were found in the apoplastic fluid of Arabidopsis thaliana. These activities acted cooperatively on xyloglucan oligosaccharides (XLFG),
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