BGLU18 (AtBG1, BGL1; At1g52400) is a glycoside hydrolase family 1 beta-glucosidase of Arabidopsis thaliana with an N-terminal signal peptide and a C-terminal ER-retention motif. It is retained in the lumen of the endoplasmic reticulum and is the main cargo of the wound- and jasmonate-inducible ER bodies and, together with PYK10/BGLU23, of the leaf ER bodies of rosette leaves. Its best-characterised activity is hydrolysis of the inactive storage conjugate abscisic acid glucose ester (ABA-GE) to free, active ABA. Dehydration triggers polymerisation of the enzyme into higher-order, more active forms and shifts it from ER bodies into the general ER, giving a rapid route to ABA that complements de novo biosynthesis. Loss of BGLU18 lowers ABA levels and impairs stomatal closure, germination control and tolerance of drought and salt stress. BGLU18 is also needed to form wound-inducible ER bodies, and with PYK10 it is required to hydrolyse the indole glucosinolate 4-methoxyindol-3-ylmethyl glucosinolate in damaged leaves, which points to a second role in ER-body-based chemical defence against herbivores.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000325 plant-type vacuole | HDA PMID:15539469 The vegetative vacuole proteome of Arabidopsis thaliana reve... | MARK AS OVER ANNOTATED | Summary: High-throughput detection in a vegetative vacuole proteome; BGLU18 is an ER-retained ER-body protein. Reason: BGLU18 carries a C-terminal ER-retention motif and every targeted localisation study places it in the ER lumen and ER bodies (PMID:19147648, PMID:30696747, PMID:31761937). The vacuole proteome entry (BGLU18 is not discussed in the cached main text) most likely reflects ER-body material co-purifying with vacuoles or ER bodies delivered to vacuoles under stress; it is not evidence that the vacuole is a site where the enzyme resides or acts. Kept as an over-annotation rather than removed because this is an experimental proteomic row. Supporting Evidence: PMID:31761937 BGLU18 is localized to the ER, whereas BGLU33 is a vacuolar enzyme. file:ARATH/BGLU18/BGLU18-uniprot.txt Prevents secretion from ER |
| GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds | IEA GO_REF:0000002 | MODIFY | Summary: Correct GH1 family-level mapping, but BGLU18 has a demonstrated specific activity. Reason: The InterPro GH1 mapping is correct but general. BGLU18 is experimentally an abscisic acid glucose ester beta-glucosidase (GO:0051993), which is a descendant of this term via beta-glucosidase activity (GO:0008422) (checked with OLS ancestors). The gene already carries GO:0051993 from experimental rows. Proposed replacements: abscisic acid glucose ester beta-glucosidase activity Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt Belongs to the glycosyl hydrolase 1 family. PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. |
| GO:0005576 extracellular region | ISM GO_REF:0000122 | REMOVE | Summary: AtSubP sequence prediction of secretion, contradicted by the ER-retention motif and by direct localisation to the ER and ER bodies. Reason: The prediction is driven by the N-terminal signal peptide alone and ignores the C-terminal ER-retention tetrapeptide (Arg-Glu-Glu-Leu) that retains BGLU18 in the ER. Immunocytochemistry and fluorescent-fusion studies place it in ER bodies and the ER, and no study reports secreted BGLU18. The extracellular ABA increase described for BGLU18 refers to the hormone it produces, not to the enzyme. This is a demonstrably wrong computational prediction. Supporting Evidence: PMID:30696747 Inducible ER bodies accumulate BGLU18, a Ξ²-glucosidase with the ER retention signal Arg-Glu-Glu-Leu PMID:19147648 BGLU18 protein was exclusively localized in ER bodies formed directly at the wounding site on cotyledons |
| GO:0005634 nucleus | HDA PMID:14617066 Analysis of the Arabidopsis nuclear proteome and its respons... | MARK AS OVER ANNOTATED | Summary: Nuclear proteome hit for an ER-lumenal, signal-peptide-bearing glycosidase. Reason: The nuclear proteome (abstract only in cache) used nuclear fractions that are commonly contaminated by ER, which is continuous with the nuclear envelope. A signal-peptide, ER-retained lumenal enzyme has no route into the nucleoplasm, and targeted studies show ER and ER-body localisation only. The row is not removed because the full text was not inspected, but it does not represent a location of BGLU18 function. Supporting Evidence: PMID:31761937 BGLU18 is localized to the ER, whereas BGLU33 is a vacuolar enzyme. |
| GO:0005634 nucleus | HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati... | MARK AS OVER ANNOTATED | Summary: Protein correlation profiling hit; same issue as the other nuclear proteomic row. Reason: BGLU18 is not discussed in the main text of this membrane-protein oligomerisation survey; any nuclear assignment comes from fractionation profiles in supplementary data. As for the other nuclear row, the ER-lumenal localisation of this ER-retained enzyme makes a nuclear location implausible. Supporting Evidence: PMID:30696747 Inducible ER bodies accumulate BGLU18, a Ξ²-glucosidase with the ER retention signal Arg-Glu-Glu-Leu |
| GO:0005777 peroxisome | HDA PMID:17951448 Proteome analysis of Arabidopsis leaf peroxisomes reveals no... | MARK AS OVER ANNOTATED | Summary: Detected in purified leaf peroxisomes; conflicts with the ER-retention signal and ER-body localisation. Reason: Reumann et al. identified BGL1 (At1g52400) in leaf peroxisome fractions and argued against artefactual co-purification of large complexes, but BGLU18 has no recognised peroxisomal targeting signal and carries an ER-retention signal, and fluorescent fusions and immunocytochemistry show ER bodies and ER only. ER bodies are dense structures that can co-sediment with peroxisomes; PYK10, the other main ER-body glucosidase, was co-detected. The peroxisome claim is not independently supported. Existing experimental row on a root organelle term - marked over-annotated, not removed. Supporting Evidence: PMID:17951448 In addition to two further glycoside hydrolases identified in leaf peroxisomes (BGL1, At1g52400; and PYK10, see Results) PMID:30696747 These results indicate that two types of Ξ²-glucosidases, BGLU18 and PYK10/BGLU23, are accumulated in L-ER bodies. |
| GO:0005783 endoplasmic reticulum | IDA PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | ACCEPT | Summary: ER localisation of AtBG1, consistent with signal peptide, ER-retention motif and later fusion-protein studies. Reason: Lee et al. localised AtBG1 to the ER in protoplasts; Han et al. confirmed ER and ER-body localisation of BGLU18 by fractionation and mRFP fusions. The ER is where the ABA-GE hydrolysis takes place. Root organelle term with direct evidence, accepted beside the ER lumen and ER body rows. Supporting Evidence: PMID:31761937 BGLU18 was originally reported to be localized to the ER of leaf protoplasts based on a constitutive overexpression study PMID:31761937 BGLU18 is localized to the ER, whereas BGLU33 is a vacuolar enzyme. |
| GO:0005788 endoplasmic reticulum lumen | IEA GO_REF:0000044 | ACCEPT | Summary: ER lumen, from UniProt subcellular location (ER-retention motif plus ER body immunolocalisation). Reason: Signal peptide, a C-terminal ER-retention motif and ER-body (lumenal, ER-derived) localisation agree that BGLU18 is a soluble lumenal ER protein. This is the sub-compartment in which the ABA-GE hydrolysis is proposed to occur. Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt Endoplasmic reticulum lumen PMID:30696747 Inducible ER bodies accumulate BGLU18, a Ξ²-glucosidase with the ER retention signal Arg-Glu-Glu-Leu |
| GO:0005975 carbohydrate metabolic process | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Generic InterPro GH1 mapping; BGLU18 acts on a hormone conjugate, not in carbohydrate metabolism. Reason: The GH1 InterPro2GO mapping assumes a role in carbohydrate metabolism. BGLU18 removes glucose from ABA-GE (and possibly a glucosinolate) to release an aglycone; the biological process is ABA metabolism and specialised metabolite activation, and glucose release is incidental. The row adds no correct biological information for this gene. Supporting Evidence: PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. |
| GO:0008422 beta-glucosidase activity | IBA GO_REF:0000033 | MODIFY | Summary: Sound family-level beta-glucosidase inheritance; BGLU18's specific activity is the ABA-GE beta-glucosidase. Reason: The PAINT node PTN000039458 spans GH1 beta-glucosidases, and BGLU18 (AT1G52400, itself among the descendant evidence) sits well inside it with both catalytic glutamates (E207, E422) annotated; E207Q abolishes activity. The inheritance is sound, but the specific activity of BGLU18 is abscisic acid glucose ester beta-glucosidase activity (GO:0051993), an is_a child of GO:0008422 (checked with OLS), already asserted on the gene by experimental rows. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: PANTHER:PTN000039458 SUPPORTS TRANSFER Deep GH1 node; the general beta-glucosidase claim holds for BGLU18, whose own experimental activity refines it to ABA-GE hydrolysis. Proposed replacements: abscisic acid glucose ester beta-glucosidase activity Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt E->Q: Loss of activity towards ABA-GE. PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. |
| GO:0008422 beta-glucosidase activity | IMP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | MODIFY | Summary: Correct but general; the paper shows hydrolysis of ABA-GE specifically. Reason: Lee et al. show that AtBG1 hydrolyses ABA-GE to free ABA and that the E207Q mutant loses this activity. The supported, more specific term is abscisic acid glucose ester beta-glucosidase activity (GO:0051993), a child of GO:0008422 that the gene already carries from the same paper. Proposed replacements: abscisic acid glucose ester beta-glucosidase activity Supporting Evidence: PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. file:ARATH/BGLU18/BGLU18-uniprot.txt E->Q: Loss of activity towards ABA-GE. |
| GO:0009414 response to water deprivation | IEP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: Dehydration induces BGLU18 and activates it by polymerisation; physiologically relevant but downstream of the core activity. Reason: BGLU18 is dehydration-inducible, dehydration triggers its polymerisation and activation, and mutants are drought-sensitive. The response context is real and well supported, but the term describes the plant's response rather than the enzyme's activity. Supporting Evidence: PMID:16990135 Dehydration rapidly induces polymerization of AtBG1, resulting in a 4-fold increase in enzymatic activity. PMID:31761937 Loss of BGLU18 delayed dehydration-induced ABA accumulation, suggesting that ABA-GE hydrolysis precedes the biosynthesis. |
| GO:0009506 plasmodesma | HDA PMID:21533090 Arabidopsis plasmodesmal proteome. | MARK AS OVER ANNOTATED | Summary: Plasmodesmal proteome hit; inconsistent with lumenal ER/ER-body localisation. Reason: Plasmodesmata contain the desmotubule (appressed ER), so cell-wall plasmodesmal preparations routinely contain ER-lumen proteins. BGLU18 is not discussed in the main text and no study shows a plasmodesmal function or enrichment for this ER-body glucosidase. Supporting Evidence: PMID:31761937 BGLU18 is localized to the ER, whereas BGLU33 is a vacuolar enzyme. |
| GO:0009507 chloroplast | HDA PMID:18431481 Sorting signals, N-terminal modifications and abundance of t... | MARK AS OVER ANNOTATED | Summary: Chloroplast proteome hit for a signal-peptide, ER-retained protein. Reason: BGLU18 has a secretory signal peptide and an ER-retention signal, not a chloroplast transit peptide, and all targeted localisations are ER/ER bodies. The high-throughput chloroplast proteome hit (BGLU18 not discussed in main text) is best treated as a contaminant. Not removed because it is an experimental row whose supplementary data was not inspected. Supporting Evidence: PMID:30696747 Inducible ER bodies accumulate BGLU18, a Ξ²-glucosidase with the ER retention signal Arg-Glu-Glu-Leu |
| GO:0009625 response to insect | IEP PMID:23144921 Water stress and aphid feeding differentially influence meta... | KEEP AS NON CORE | Summary: BGL1 transcript was down-regulated by aphid feeding in a qRT-PCR panel. Reason: Mewis et al. report that BGL1 (used as a JA-responsive marker; BGL1 is a synonym of BGLU18 and the gene mapping in the supplementary primer table was not inspected) was down-regulated by feeding of two aphid species. This is a genuine expression response to insects, and it fits the separate evidence that BGLU18-containing ER bodies defend leaves against chewing herbivores (PMID:30696747). It is peripheral to the enzyme's core role. Supporting Evidence: PMID:23144921 BGL1, commonly induced by JA, was down-regulated after feeding by either M. persicae or B. brassicae in all water treatments. |
| GO:0009651 response to salt stress | IEP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: Salt induces BGLU18 expression; mutants show abiotic stress sensitivity. Reason: UniProt (curated from PMID:16990135) records induction by salt, and the paper reports abiotic-stress-sensitive mutants. Physiological context of the ABA-releasing activity, not the core function. Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt By ABA, dehydration, wounding and salt treatment. PMID:16990135 Loss of AtBG1 causes defective stomatal movement, early germination, abiotic stress-sensitive phenotypes, and lower ABA levels |
| GO:0009687 abscisic acid metabolic process | IDA PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | ACCEPT | Summary: BGLU18 directly converts ABA-GE into free ABA, a step of ABA metabolism. Reason: The enzyme catalyses the deconjugation step that releases active ABA from its glucose ester; this is the process in which the core activity participates. GO has no specific term for ABA-GE hydrolysis, and ABA biosynthetic process (GO:0009688) is defined around formation of ABA by de novo synthesis, so the metabolic-process parent is the appropriate precision. Supporting Evidence: PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. PMID:31761937 Collectively, these results uncover a direct relationship between ER body number and BGLU18-mediated ABA-GE hydrolysis activity. |
| GO:0009737 response to abscisic acid | IEP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: BGLU18 expression is induced by ABA. Reason: ABA induction of BGLU18 is recorded by UniProt from the cited paper. The term records an expression response, not the enzyme's role, and is kept as non-core context. Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt By ABA, dehydration, wounding and salt treatment. |
| GO:0009789 positive regulation of abscisic acid-activated signaling pathway | IMP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: By releasing free ABA, BGLU18 increases ABA signalling output; mutants have lower ABA and ABA-deficient phenotypes. Reason: The mutant phenotype (lower ABA, defective stomatal closure, early germination) shows that BGLU18 raises ABA-dependent signalling by supplying ligand. The effect is real and is the physiological purpose of the activity, but it acts through ligand supply rather than through the signalling machinery, so it is kept as non-core. Supporting Evidence: PMID:16990135 Loss of AtBG1 causes defective stomatal movement, early germination, abiotic stress-sensitive phenotypes, and lower ABA levels file:ARATH/BGLU18/BGLU18-uniprot.txt The ABA produced by BGLU18 contributes to the initiation of intracellular |
| GO:0010119 regulation of stomatal movement | IMP PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: bglu18 mutants show defective stomatal closure. Reason: Defective stomatal movement in loss-of-function plants is a downstream consequence of reduced ABA supply. A valid phenotype-based process row, but not the core function. Supporting Evidence: PMID:16990135 Loss of AtBG1 causes defective stomatal movement |
| GO:0010168 ER body | IDA PMID:19147648 Constitutive and inducible ER bodies of Arabidopsis thaliana... | ACCEPT | Summary: Immunocytochemistry places BGLU18 in wound-inducible ER bodies; later confirmed in leaf ER bodies. Reason: Directly shown by immunocytochemistry (PMID:19147648) and BGLU18-TagRFP imaging (PMID:30696747); BGLU18 is one of the two most abundant ER body proteins. Supporting Evidence: PMID:19147648 BGLU18 protein was exclusively localized in ER bodies formed directly at the wounding site on cotyledons PMID:34110257 PYK10 (BGLU23) and BGLU18 are the most abundant ER body proteins. |
| GO:0019762 glucosinolate catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Inherited from PEN2 and PYK10; consistent with the bglu18 pyk10 double-mutant defect in 4MI3G hydrolysis. Reason: The PAINT node PTN002570733 groups the ER-body/defence GH1 clade (PEN2/BGLU26, PYK10). For BGLU18 the inheritance is supported by its own data - the bglu18 pyk10 double mutant fails to hydrolyse 4-methoxyindol-3-ylmethyl glucosinolate in damaged leaves - although the double mutant cannot separate the two enzymes and a direct glucobrassicin role was not confirmed (PMID:36388588). A secondary, defence-related role beside ABA-GE hydrolysis. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002570733 SUPPORTS TRANSFER BGLU18-specific double-mutant data agree with the inherited claim. Supporting Evidence: PMID:30696747 These results suggest that 4MI3G is hydrolyzed by BGLU18 and/or PYK10, but not by TGG1 and TGG2 PMID:36388588 However, the certain involvement of BGLU18 in the breakdown of glucosinolates could not be demonstrated |
| GO:0042802 identical protein binding | IPI PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: AtBG1 self-associates into high-molecular-weight polymers upon dehydration; the With/From field names a different locus. Reason: Self-association of AtBG1 is the basis of its stress-induced activation, so identical protein binding is true of BGLU18 and relevant to its regulation, though not its catalytic core. The With/From value AGI_LocusCode:AT1G54200 is a different locus; for a homomeric interaction it should be AT1G52400 itself, and 54200/52400 is a digit transposition. Recorded as a source defect. Supporting Evidence: PMID:16990135 Dehydration rapidly induces polymerization of AtBG1, resulting in a 4-fold increase in enzymatic activity. |
| GO:0050832 defense response to fungus | IEP PMID:19656045 Disease-specific expression of host genes during downy milde... | MODIFY | Summary: Expression induced during compatible infection by the oomycete Hyaloperonospora arabidopsidis; not a fungus, and not a defence response. Reason: The study reports genes induced during compatible (susceptible) but not incompatible interactions with downy mildew, an oomycete. Expression induction supports a response term, not a defence term, and the stimulus is an oomycete. The paper (abstract only) is accepted as the source of BGLU18 induction, but the term should be response to oomycetes (GO:0002239, same aspect). Recorded as a source defect. Proposed replacements: response to oomycetes Supporting Evidence: PMID:19656045 induced during compatible but not during incompatible interactions with the downy mildew pathogen Hyaloperonospora arabidopsidis |
| GO:0051258 protein polymerization | IDA PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | KEEP AS NON CORE | Summary: Dehydration-induced polymerisation of AtBG1 activates the enzyme. Reason: Directly shown; the protein polymerises with itself, which is a regulatory mechanism of the core activity rather than a function in its own right. Supporting Evidence: PMID:16990135 Dehydration rapidly induces polymerization of AtBG1, resulting in a 4-fold increase in enzymatic activity. |
| GO:0051993 abscisic acid glucose ester beta-glucosidase activity | EXP PMID:17923167 Effect of ABA-beta-D-glucopyranosyl ester and activity of AB... | ACCEPT | Summary: Correct activity for BGLU18; the cited paper characterises ABA-GE glucosidase activity in crude seedling extracts. Reason: The activity is independently established for BGLU18 (PMID:16990135, E207Q mutant). The cited abstract measures ABA-beta-D-glucosidase activity in crude extracts of seedlings, and UniProt takes its kinetic constants for BGLU18 from it; whether BGLU18 itself was assayed cannot be checked from the abstract. The function is accepted on the combined evidence. Supporting Evidence: PMID:17923167 The pH optimum of this enzyme in crude extract of Arabidopsis seedlings was 6.0 PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. |
| GO:0051993 abscisic acid glucose ester beta-glucosidase activity | IDA PMID:16990135 Activation of glucosidase via stress-induced polymerization ... | ACCEPT | Summary: Core activity - hydrolysis of ABA-GE to free ABA. Reason: Lee et al. demonstrated ABA-GE hydrolysis by AtBG1, abolished by the E207Q catalytic mutation, and in planta activity was later confirmed with bglu18 as background control (PMID:31761937). Supporting Evidence: PMID:16990135 Here we report that AtBG1, a beta-glucosidase, hydrolyzes glucose-conjugated, biologically inactive ABA to produce active ABA. file:ARATH/BGLU18/BGLU18-uniprot.txt E->Q: Loss of activity towards ABA-GE. |
| GO:0051993 abscisic acid glucose ester beta-glucosidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic mapping from the curated Rhea/EC reaction; correct. Reason: The UniProt catalytic-activity record (RHEA:31347, EC 3.2.1.175) is curated from experimental work and matches the core activity. Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt Hydrolyzes abscisic acid glucose ester (ABA-GE) which |
| GO:0071472 cellular response to salt stress | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Inherited from BGLU21/BGLU22; BGLU18 is salt-induced and mutants are stress-sensitive. Reason: The PAINT seeds are the root ER-body glucosidases BGLU21 and BGLU22. For BGLU18 the claim is consistent with its own salt induction and abiotic-stress phenotypes, so the inheritance holds, but it is a physiological context of ABA release rather than the enzyme's core role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002570733 SUPPORTS TRANSFER Consistent with BGLU18's own salt-induction and stress-phenotype data. Supporting Evidence: file:ARATH/BGLU18/BGLU18-uniprot.txt By ABA, dehydration, wounding and salt treatment. PMID:16990135 abiotic stress-sensitive phenotypes |
| GO:0080119 ER body organization | IMP PMID:19147648 Constitutive and inducible ER bodies of Arabidopsis thaliana... | KEEP AS NON CORE | Summary: bglu18 knockouts do not form wound-inducible ER bodies; L-ER bodies are also lost in bglu18 pyk10. Reason: BGLU18 is the bulk cargo of inducible ER bodies and its loss abolishes their formation, so it contributes structurally to the organelle (as PYK10 does for constitutive ER bodies). Supported by two independent studies, but secondary to its enzymatic role. Supporting Evidence: PMID:19147648 ER bodies were not induced in locally and systemically wounded cotyledons of the bglu18 knock-out mutant PMID:30696747 No L-ER bodies were observed in the three types of epidermal cells in the bglu18 pyk10 mutant |
| GO:0098542 defense response to other organism | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Inherited from PEN2; consistent with ER-body defence against herbivores. Reason: The seed is PEN2 (BGLU26). For BGLU18, the L-ER bodies it forms with PYK10 protect leaves against isopod herbivory, so a defence role holds for the gene, as a secondary role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002570733 SUPPORTS TRANSFER Consistent with BGLU18/PYK10 double-mutant herbivory data. Supporting Evidence: PMID:30696747 A subsequent feeding assay with the terrestrial isopod Armadillidium vulgare revealed that bglu18 pyk10 leaves were severely damaged as a result of herbivory. |
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Download this section (compressed HTML)Q: Does purified BGLU18 hydrolyse 4-methoxyindol-3-ylmethyl glucosinolate or other glucosinolates, or is the 4MI3G defect of bglu18 pyk10 attributable to PYK10 alone?
Q: Is the With/From partner AT1G54200 on the identical protein binding row (PMID:16990135) a transposition of AT1G52400?
Q: How does ABA-GE, which is stored mainly in the vacuole and apoplast, reach BGLU18 in the ER lumen under dehydration?
Experiment: Express and purify BGLU18 and PYK10 separately and measure kinetics on ABA-GE, 4MI3G and glucobrassicin; compare bglu18 and pyk10 single mutants for 4MI3G breakdown in leaf homogenates.
Hypothesis: BGLU18 has intrinsic thioglucosidase (myrosinase) activity on 4MI3G.
Experiment: Identify interface residues needed for polymerisation and test non-polymerising variants for ABA-GE hydrolysis and dehydration-induced ABA accumulation in bglu18 complemented lines.
Hypothesis: Polymerisation is required for stress activation of BGLU18 in planta.
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