Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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The nucleotide sequence of an 852 base pair (bp) DNA fragment containing the entire gene coding for thermostable beta-1,3-1,4-glucanase of Bacillus macerans has been determined. The bglM gene comprises an open reading frame (ORF) of 711 bp (237 codons) starting with ATG at position 93 and extending to the translational stop codon TAA at position 804. The deduced amino acid sequence of the mature protein shows 70% homology to published sequences of mesophilic beta-1,3-1,4-glucanases from B. subtilis and B. amyloliquefaciens. The sequence coding for mature beta-glucanase is preceded by a putative signal peptide of 25 amino acid residues, and a sequence resembling a ribosome-binding site (GGAGG) before the initiation codon. By contrast with the processed protein, the N-terminal amino acid sequence constituting the putative leader peptide bears no or only weak homology to signal peptides of mesophilic Bacillus endo-beta-glucanases. The B. macerans signal peptide appears to be functional in exporting the enzyme to the periplasm in E. coli. More than 50% of the whole glucanase activity was localized in the periplasmic space and in the supernatant. Whereas homology to endo-1,4-beta-glucanases is completely lacking, a weak amino acid homology between the sequence surrounding the active site of phage T4 lysozyme and a sequence spanning residues 126 through 161 of B. macerans endo-beta-glucanase could be identified.
Mol Gen Genet 1990 Jul
PMID:Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases. 227 30

Eggs of the sea urchin Strongylocentrotus purpuratus were fertilized in normal and in several chloride-deficient sea waters ([ Cl-]: normal greater than isethionate greater than methyl sulfonate greater than bromide). The fertilization envelopes (FE) were thinner and failed to harden, and the characteristic I-T transition did not occur. The permeability of the experimental FEs, as determined by release of protein from the perivitelline space, increased in the order of decreasing [Cl-]. Release of the enzymes beta-1,3-glucanase and cortical granule protease were not significantly altered. On the other hand, release of ovoperoxidase was increased three to four times in bromide sea water. Furthermore, a dose-response was observed in varying concentrations of bromide-normal sea water. With decreasing chloride (increasing bromide) concentration, more ovoperoxidase activity was observed. Cytochemical localization of ovoperoxidase activity with diaminobenzidine revealed almost a total lack of staining of FEs from bromide-substituted sea water. The results suggest that in chloride-deficient sea waters protein incorporation into the nascent FE is impaired. At least in the case of bromide, the incorporation of ovoperoxidase into the nascent FE was also inhibited.
Mol Reprod Dev 1990 Feb
PMID:Fertilization envelope assembly in sea urchin eggs inseminated in chloride-deficient sea water: II. Biochemical effects. 231 May 68

The endo-beta-1,3-1,4-glucanase enzyme of Bacillus subtilis C120, when synthesized in Escherichia coli, is located mainly in the cytoplasm, but enzyme activity is also detected in the periplasmic space and in the extracellular medium. The proportion recovered in the extracellular medium is not altered by changes in the levels of synthesis of the enzyme. Lysis of E. coli cells is ruled out as the cause of the secretion by the normal localization of beta-galactosidase, an intracellular protein. However, beta-lactamase, which is normally found in the periplasmic space, is detected in the extracellular medium of E. coli transformants containing beta-glucanase plasmids, suggesting that the presence of beta-glucanase in the cell alters the permeability of the outer membrane. The beta-glucanase proteins found in the extracellular medium, the periplasmic space and the cytoplasm have the same electrophoretic mobilities as the secreted enzyme of B. subtilis. Amino-terminal sequencing has shown that the beta-glucanase enzyme in the intracellular fraction of E. coli is processed at a site two amino acids distant from the processing site used in B. subtilis.
Mol Microbiol 1988 Nov
PMID:Secretion and processing of the Bacillus subtilis endo-beta-1,3-1,4-glucanase in Escherichia coli. 314 87

Clones encoding beta-1,3-glucanase have been isolated from a Hevea cDNA library prepared from the latex of Hevea brasiliensis using a probe Nicotiana plumbaginifolia cDNA encoding beta-1,3-glucanase, gnl. Nucleotide sequence analysis showed that a 1.2 kb Hevea cDNA encoding a basic beta-1,3-glucanase showed 68% nucleotide homology to gnl cDNA. Northern blot analysis using the Hevea cDNA as probe detected a mRNA of 1.3 kb which was expressed at higher levels in latex than in leaf. In situ hybridization analysis using petiole sections from Hevea localized the beta-1,3-glucanase mRNA to the laticifer cells. Genomic Southern analysis suggested the presence of a low-copy gene family encoding beta-1,3-glucanases in H. brasiliensis.
Plant Mol Biol 1995 Oct
PMID:beta-1,3-Glucanase is highly-expressed in laticifers of Hevea brasiliensis. 757 90

Purified lipopolysaccharide (LPS) from Xanthomonas campestris pv. campestris induced accumulation of transcript for beta-1,3-glucanase in turnip at concentrations of 1 micrograms/ml. The lipid A-inner core structure was required for activity but the O-antigen had no role. We suggest that release of LPS in planta triggers expression of at least some defense-related genes.
Mol Plant Microbe Interact
PMID:Lipopolysaccharide from Xanthomonas campestris induces defense-related gene expression in Brassica campestris. 757 22

We have studied the induction of beta-1,3-glucanase (BGL) in turnip following inoculation with pathovars of Xanthomonas campestris and derived mutants. BGL transcript accumulated more rapidly in leaves in the incompatible interactions with X. c. pv. armoraciae and X. c. pv. raphani than in the compatible interaction with X. c. pv. campestris. No accumulation was seen in response to wounding or inoculation with water, salicylic acid, or Escherichia coli. Deletion of the hrp cluster from the X. campestris pathovars caused a reduction in the level of transcript accumulation; these effects were much more pronounced in the incompatible than in the compatible interaction, in which bacterial growth was also affected. In the compatible interaction, bacterial growth and BGL transcript accumulation were not altered by mutation of bacterial genes involved in the regulation of the synthesis of extracellular enzymes or their export from the cell, or by mutation of the structural genes for extracellular endoglucanase and serine protease. Mutation of genes involved in the synthesis of extracellular polysaccharide or lipopolysaccharide reduced bacterial survival in planta, so that the numbers were between two and three orders of magnitude lower than the number of wild-type bacteria. However, total BGL transcript accumulation after inoculation with these mutants was about 80% of that seen after inoculation with the wild-type bacteria, suggesting that one aspect of the role of extracellular polysaccharide and lipopolysaccharide in pathogenesis is to mask the presence of bacteria in the plant. Our results are discussed in the context of work on other plant-microbe interactions.
Mol Plant Microbe Interact
PMID:Defense-related gene induction in Brassica campestris in response to defined mutants of Xanthomonas campestris with altered pathogenicity. 794 24

The class I beta-1,3-glucanases are antifungal vacuolar proteins implicated in plant defense that show developmental, hormonal, and pathogenesis-related regulation. The tobacco enzymes are encoded by a small gene family with members derived from ancestors related to the present-day species Nicotiana sylvestris and N. tomentosiformis. We studied the expression in transgenic tobacco plants of a chimeric beta-glucuronidase (GUS) reporter gene fused to 1.6 kb of upstream sequence of the tobacco class I beta-1,3-glucanase B (GLB) gene, which is of N. tomentosiformis origin. Expression of the GUS reporter gene and the accumulation of class I beta-1,3-glucanase and its mRNA showed very similar patterns of regulation. In young seedlings the reporter gene was expressed in the roots. In mature tobacco plants it was preferentially expressed in lower leaves and roots and was induced in leaves by ethylene treatment and by infection with tobacco mosaic virus (TMV). Furthermore, it was down-regulated in cultured leaf discs by combinations of the hormones auxin and cytokinin. Histological studies of GUS activity showed that the GLB promoter shows highly localized expression in roots of seedlings. It is also expressed in a ring of cells around necrotic lesions induced by TMV infection, but not in cells immediately adjacent to the lesions or in the lesions themselves. The results of deletion analyses suggest that multiple positive and negative elements in the GLB promoter regulate its activity. The region from -1452 to -1193 containing two copies of the heptanucleotide AGCCGCC, which is highly conserved in plant-stress and defense-related genes, is necessary for high level expression in leaves. Additional regions important for organ-specific and regulated expression were: -568 to -402 for ethylene induction of leaves; -402 to -211 for expression in lower leaves and cultured leaf discs and for TMV induction of leaves; and -211 to -60 for expression in roots.
Plant Mol Biol 1994 May
PMID:Developmental, hormonal, and pathogenesis-related regulation of the tobacco class I beta-1,3-glucanase B promoter. 801 77

beta-1,3-glucanases are hydrolytic enzymes considered to constitute part of the general array of defense genes induced by pathogen infection in higher plants. We have isolated and characterized two complementary DNA clones, corresponding to new beta-1,3-glucanases from tomato plants (Lycopersicon esculentum) which are expressed upon challenge with citrus exocortis viroid. Amino acid sequence comparison revealed that they are most similar to beta-1,3-glucanases from tobacco, particularly to PR-Q', the unique component of the class III beta-1,3-glucanase. The deduced amino acid sequences of the two tomato beta-1,3-glucanases indicate that, although being highly similar in amino acid sequence, they have different isoelectric points: pI 10.5 for the basic isoform (Tom PR-Q'b) and pI 5.2 for the acidic one (Tom PR-Q'a). The expression of these two beta-1,3-glucanase messenger RNAs (mRNAs) in response to viroid infection and ethephon treatments was examined. mRNAs for these two isoforms are coordinately expressed and induced similarly to mRNAs for other PR proteins, indicating that they are part of a general and coordinate mechanism of response of tomato plants susceptible to viroid infection.
Plant Mol Biol 1994 Mar
PMID:Genes encoding acidic and basic class III beta-1,3-glucanases are expressed in tomato plants upon viroid infection. 819 97

A critical stage in pollen development is the dissolution of the four products of meiosis, the tetrads, into free microspores. The tetrads are surrounded by a thick callose wall composed of beta-1,3-glucan. At the completion of meiosis, the tetrads are released into the anther locule after hydrolysis of the callose by a beta-1,3-glucanase. Using the polymerase chain reaction, we have amplified and subsequently cloned a cDNA corresponding to a beta-1,3-glucanase, tobacco (Nicotiana tabacum cv. Samsun) anther glucanase (Tag 1), which is expressed exclusively in anthers from meiosis to the free microspore stage of pollen development. The identity of the clone was determined by DNA and deduced protein sequence similarity to other known beta-1,3-glucanases. Several regions strictly conserved among four classes of glucanases are also conserved in the Tag 1 protein. Tag 1 represents a novel class of beta-1,3-glucanase based on phylogenetic analysis and RNA expression pattern. Tag 1 RNA was detected in situ only in the tapetum, with maximal expression just prior to tetrad dissolution. Due to its expression pattern and sequence similarity to other beta-1,3-glucanases, we believe Tag 1 may be involved in tetrad dissolution.
Plant Mol Biol 1994 Mar
PMID:Cloning and characterization of Tag 1, a tobacco anther beta-1,3-glucanase expressed during tetrad dissolution. 820 27

We show that a 61 bp fragment derived from the promoter region of the tobacco class I beta-1,3-glucanase GLB gene enhances transcription in Nicotiana plumbaginifolia protoplasts independent of orientation relative to the start of transcription. This fragment leads to a cooperative stimulation of transcription when combined with the cauliflower mosaic virus 35S as-1 enhancer element. The GLB enhancer contains two copies of the sequence AGCCGCC, which is conserved in several genes showing expression patterns similar to the GLB gene, as well as a sequence identical at 6 of 7 bp. Point mutations in these three sequences eliminate the enhancer activity of the 61 bp fragment. Nuclear extracts prepared from leaves of tobacco plants contain one or more putative transcription factors that interact specifically with the GLB enhancer. This factor was much less abundant in nuclear extracts prepared from upper leaves of untreated tobacco plants than in nuclear extracts prepared from upper leaves of ethylene-treated plants or from lower leaves. Since beta-1,3-glucanase genes are expressed at very low levels in upper leaves of tobacco plants, at higher levels in lower leaves, and are induced in all leaves after treatment of plants with the stress hormone ethylene, we conclude that the enhancer element interacts with one or more transcription factors whose binding activity is correlated with gene expression in vivo.
Plant Mol Biol 1993 Jan
PMID:A 61 bp enhancer element of the tobacco beta-1,3-glucanase B gene interacts with one or more regulated nuclear proteins. 842 42


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