Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Infection of tobacco by tobacco mosaic virus (TMV) induces coordinate expression of genes encoding acidic and basic beta-1,3-glucanase isoforms. These genes are differentially expressed in response to other treatments. Salicylate treatment induces acidic glucanase mRNA to a higher level than basic glucanase mRNA. Ethylene treatment and wounding strongly induce the basic glucanase genes but have little effect on genes encoding the acidic isoforms. Furthermore, the basic glucanase genes are constitutively expressed in roots and lower leaves of healthy plants, whereas the acidic glucanase genes are not. In order to investigate how these expression patterns are established, we fused promoter regions of an acidic and a basic glucanase gene to the beta-glucuronidase (GUS) reporter gene and examined expression of these constructs in transgenic tobacco plants. A fragment of 1750 bp and two 5'-truncated fragments of 650 bp and 300 bp of the acidic glucanase promoter were tested for induction of GUS gene expression after salicylate treatment and TMV infection. Upstream sequences of 1750 bp and 650 bp were sufficient for induction of the reporter gene by salicylate treatment and TMV infection, but the activity of the 300 bp fragment was strongly reduced. The results suggest that the 1750 bp upstream sequence of the acidic glucanase gene contains multiple regulatory elements. For the basic glucanase promoter it is shown that 1476 bp of upstream sequences were able to drive expression in response to TMV infection and ethylene treatment, but no response was found to incision wounding. Furthermore, high GUS activity was found in lower leaves and roots of healthy transgenic plants, carrying the 1476 bp basic glucanase promoter/GUS construct. When the promoter was truncated up to position -446 all activity was lost, indicating that the region between -1476 and -446 of the basic glucanase promoter is necessary for organ-specific and developmentally regulated expression as well as for induced expression in response to infection and other stress treatments.
Plant Mol Biol 1993 Feb
PMID:Analysis of regulatory elements involved in stress-induced and organ-specific expression of tobacco acidic and basic beta-1,3-glucanase genes. 844 40

A barley acidic beta-1,3-glucanase gene was recovered from a barley genomic library by homology with a partial cDNA of barley basic beta-1,3-glucanase isoenzyme GII. The gene, Abg2, is homologous to the PR2 family of pathogenesis-related beta-1,3-glucanase genes. The ABG2 protein has 81% amino acid similarity to barley basic beta-1,3-glucanase GII. The ABG2 protein is encoded as a preprotein of 336 amino acids including a 28 amino acid signal peptide. A 299 bp intron occurs within codon 25. The mature ABG2 protein has a predicted mass of 32,642 Da and a calculated isoelectric point of 4.9. The second exon of the Abg2 gene shows a strong preference for G + C in the third position of degenerate codons. The Abg2 gene was functionally expressed in Escherichia coli. Abg2 mRNA is constitutively expressed in barley root; leaf expression of Abg2 mRNA is induced by mercuric chloride and infection by Erysiphe graminis f. sp. hordei. Southern blot analysis indicates that Abg2 is a member of a small gene family.
Plant Mol Biol 1993 May
PMID:Structure and expression of a barley acidic beta-glucanase gene. 850 35

An acidic beta-1,3-glucanase was detected in cucumber leaves inoculated with either Colletotrichum lagenarium or tobacco necrosis virus (TNV) as well as in the leaves above those inoculated with the pathogens. The enzyme is extracellular and migrates in native polyacrylamide gel electrophoresis (PAGE) together with a Class III chitinase, a bifunctional chitinase/lysozyme. The beta-1,3-glucanase was separated by ultra-narrow pH range IEF-PAGE or by SDS_PAGE and was purified to apparent homogeneity. Only one isoform of the enzyme was detected. Its apparent molecular mass in 38 kDa as estimated by SDS-PAGE, its isoelectric point is 3.6 and the specific activity is approximately 26 micromol glucose equivalents liberated from laminarin min(-1)mg(-1) protein. Partial amino acid (five peptide fragments with a total of 65 amino acids) sequencing of the beta-1,3-glucanase revealed similarities of 49% to 72% to sequences of published beta-1,3-glucanases from tobacco, tomato, soybean, barley, and rice plants. A time course study indicated that the increase of the beta-1,3-glucanase activity was associated with induced resistance against C. lagenarium. The implications of these results to coordinate defense responses in plant-microbe interactions are discussed.
Mol Plant Microbe Interact
PMID:Purification and characterization of an acidic beta-1,3-glucanase from cucumber and its relationship to systemic disease resistance induced by Colletotrichum lagenarium and tobacco necrosis virus. 866

A gene which codes for a thermostable endo beta-1,3-glucanase (EC 3.2.1.39) from a Gram positive anaerobic thermophilic bacteria Clostridium thermocellum F7, was fused to 35S promoter and polyadenylation signal of Cauliflower Mosaic Virus (CaMV) strain Cabb B-D. This chimaeric gene fusion was introduced into Nicotiana plumbaguinifolia protoplasts using PEG-mediated DNA transfer method of transformation. Transient expression of the thermostable endo beta-1,3-glucanase was carried out in the protoplasts and was assayed at 70 degrees C pH 8.0, suggesting that the chimaeric gene fusion: (i) is correctly transcribed and translated in plant cells; (ii) the product of translation (the thermostable endo beta-1,3-glucanase protein) is easy to assay since most of the plants' enzymes have their optimal reaction temperature at 40-60 degrees C and at neutral or weak-acidic condition which is a characteristic of plant cells; (iii) can be used as a model for studying and understanding some of the mechanisms of plant defence systems at the enzyme protein level, in case of stress conditions.
Mol Gen Mikrobiol Virusol 1997
PMID:Expression of a bacterial endo beta-1,3-glucanase gene under the control of CAMV 35S promoter in Nicotiana plumbaguinifolia protoplasts. 904 96

Expression of a beta-1,3-glucanase transgene (gn1) driven by the CaMV 35S promoter is silenced in the T17 homozygous tobacco transgenic line. This silencing process is post-transcriptionally regulated and subject to developmental control. We have examined this phenomenon to investigate the developmental pathways involved in suppression and reactivation of gn1 expression as well as to identify the plant tissues where these processes occur. Analysis of beta-1,3-glucanase activity and gene expression have allowed us to determine that suppression of gn1 is a very efficient process reducing the steady-state gn1 mRNA level, simultaneously, in all leaves of the plant. Gene silencing occurs a few weeks after seed germination, and is maintained throughout vegetative growth and floral development. Expression of gn1 is restored in the maturing fruit some time after fertilization. In situ hybridization analyses show that expression of gn1 is restored within the developing seeds in tissues derived from meiotically divided cells. In contrast to the high level of expression found in seedlings obtained from germinated T17 homozygous seeds, the expression of gn1 is not reactivated in plantlets regenerated in vitro from leaf explants of suppressed T17 homozygous plants that is, in plant tissues obtained by mitotic division. Thus, reactivation of gn1 expression specifically occurs along the developmental programme controlling sexual reproduction and likely throughout epigenetic modifications affecting the state of gene expression during meiosis.
Plant Mol Biol 1997 May
PMID:Silencing of a beta-1,3-glucanase transgene is overcome during seed formation. 917 19

Inoculation of soybean (Glycine max L. cv. Jangyup) hypocotyls with Phytophthora sojae f. sp. glycines results in a marked accumulation of some pathogenesis-related (PR) proteins. A basic beta-1,3-glucanase (34 kDa) was purified from soybean hypocotyls infected by an incompatible race of P. sojae f. sp. glycines using CM-cellulose cation exchange chromatography and Bio-gel P-60 gel filtration. The purified soybean beta-1,3-glucanase cross-reacted with polyclonal antibody raised against a tomato beta-1,3-glucanase. The activity of beta-1,3-glucanase was much higher in the infected soybean hypocotyls than the healthy ones. The beta-1, 3-glucanase purified from soybean inhibited spore germination and hyphal growth of the chitin-negative fungus P. sojae f. sp. glycines, but did not show any antifungal activity against the chitin-containing fungi Alternaria mali, Colletotrichum gloeosporioides, and Magnaporthe grisea.
Mol Cells 1997 Jun 30
PMID:Purification and antifungal activity of a basic 34 kDa beta-1,3-glucanase from soybean hypocotyls inoculated with Phytophthora sojae f. sp. glycines. 926 30

We report here cloning from the marine gliding bacterium Cytophaga drobachiensis of kappa-carrageenase, a glycoside hydrolase involved in the degradation of kappa-carrageenan. Structural features in the nucleotide sequence are pointed out, including the presence of an octameric omega sequence similar to the ribosome-binding sites of various eukaryotes and prokaryotes. The cgkA gene codes for a protein of 545 aa, with a signal peptide of 35 aa and a 229-aa-long posttranslationaly processed C-terminal domain. The enzyme displays the overall folding and catalytic domain characteristics of family 16 of glycoside hydrolases, which comprises other beta-1,4-alpha-1,3-D/L-galactan hydrolases, beta-1,3-D-glucan hydrolases (laminarinases), beta-1,4-1,3-D-glucan hydrolases (lichenases), and beta-1,4-D-xyloglucan endotransglycosylases. In order to address the origin and evolution of CgkA, a comprehensive phylogenetic tree of family 16 was built using parsimony analysis. Family-16 glycoside hydrolases cluster according to their substrate specificity, regardless of their phylogenetic distribution over eubacteria and eukaryotes. Such a topology suggests that the general homology between laminarinases, agarases, kappa-carrageenases, lichenases, and xyloglucan endotransglycosylases has arisen through gene duplication, likely from an ancestral protein with laminarinase activity.
Mol Biol Evol 1998 May
PMID:The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases. 958 Sep 81

Open reading frames in the genome of Saccharomyces cerevisiae were screened for potential glycosylphosphatidylinositol (GPI)-attached proteins. The identification of putative GPI-attached proteins was based on three criteria: the presence of a GPI-attachment signal sequence, a signal sequence for secretion and a serine- or threonine-rich sequence. In all, 53 ORFs met these three criteria and 38 were further analyzed as follows. The sequence encoding the 40 C-terminal amino acids of each was fused with the structural gene for a reporter protein consisting of a secretion signal, alpha-galactosidase and a hemagglutinin (HA) epitope, and examined for the ability to become incorporated into the cell wall. On this basis, 14 of fusion proteins were classified as GPI-dependent cell wall proteins because cells expressing these fusion proteins: (i) had high levels of alpha-galactosidase activity on their surface; (ii) released significant amounts of the fusion proteins from the membrane on treatment with phosphatidylinositol-specific phospholipase C (PI-PLC); and (iii) released fusion proteins from the cell wall following treatment with laminarinase. Of the 14 identified putative GPI-dependent cell wall proteins, 12 had novel ORFs adjacent to their GPI-attachment signal sequence. Amino acid sequence alignment of the C-terminal sequences of the 12 ORFs, together with those of known cell wall proteins, reveals some sequence similarities among them.
Mol Gen Genet 1998 Apr
PMID:Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae. 961 72

To understand the coordinated functions of the different classes of defense-related genes expressed in plant disease resistance, the expression patterns of pathogenesis related (PR) protein genes and genes involved in antioxidation and the production of secondary metabolites were examined. The expression patterns of the respective defense-related genes were monitored following TMV infection or salicylic acid treatment. Northern blot analyses showed that PR genes such as PR-1, beta-1,3-glucanase and chitinase were strongly induced in tobacco leaves upon TMV infection or salicylic acid treatment. 3-Hydroxy-3-methylglutaryl CoA reductase (HMGR) and phenylalanine ammonialyase (PAL), involved in isoprenoid and phenylpropanoid biosynthesis, respectively, were mildly induced at the late stage of normal hypersensitive response (HR) or after salicylic acid treatment when compared with the PR-gene expressions. However, in acute HR, they were strongly expressed at the early stage. Interestingly, the expression of the antioxidative genes, anionic peroxidase and ascorbate peroxidase, were inversely expressed following TMV infection and salicylic acid treatment. Differential expression of 3 groups of genes involved in plant defense responses are discussed in relation to different signal transduction pathways.
Mol Cells 1998 Aug 31
PMID:Coordinated expression of defense-related genes by TMV infection or salicylic acid treatment in tobacco. 974 24

Class I beta-1,3-glucanase (betaGLU I) is transcriptionally induced in the micropylar endosperm just before its rupture prior to the germination (i.e. radicle emergence) of Nicotiana tabacum L. cv. 'Havana 425' seeds. Ethylene is involved in endosperm rupture and high-level betaGLU I expression; but, it does not affect the spatial and temporal pattern of betaGLU I expression. A promoter deletion analysis of the tobacco betaGLU I B gene suggests that (1) the distal - 1452 to - 1193 region, which contains the positively acting ethylene-responsive element (ERE), is required for high-level, ethylene-sensitive expression, (2) the regions - 1452 to - 1193 and -402 to 0 contribute to downregulation by abscisic acid (ABA), and (3) the region -402 to -211 is necessary and sufficient for low-level micropylar-endosperm-specific expression. Transcripts of the ERE-binding proteins (EREBPs) showed a novel pattern of expression during seed germination: light or gibberellin was required for EREBP-3 and EREBP-4 expression; EREBP-4 expression was constitutive and unaffected by ABA or ethylene; EREBP-3 showed transient induction just before endosperm rupture, which was earlier in ethylene-treated seeds and inhibited by ABA. No expression of EREBP- and EREBP-2 was detected. In contrast to betaGLU I, EREBP-3 and EREBP-4 were not expressed specifically in the micropylar endosperm. The results suggest that transcriptional regulation of betaGLU I could depend on: activation of ethylene signalling pathways acting via EREBP-3 with the ERE as the target, and ethylene-independent signalling pathways with targets in the proximal promoter region that are likely to determine spatial and temporal patterns of expression.
Plant Mol Biol 1998 Nov
PMID:Ethylene-responsive element binding protein (EREBP) expression and the transcriptional regulation of class I beta-1,3-glucanase during tobacco seed germination. 986 96


<< Previous 1 2 3 4 5 6 7 8 Next >>