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)

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

A (1-->3)-beta-D-glucan 3-glucanohydrolase (EC 3.2.1.39) of apparent M(r) 32,000, designated GII, has been purified from germinated barley grain and characterized. The isoenzyme is resolved from a previously purified isoenzyme (GI) on the basis of differences in their isoelectric points; (1-->3)-beta-glucanases GI and GII have pI values of 8.6 and > or = 10.0, respectively. Comparison of the sequences of their 40 NH2-terminal amino acids reveals 68% positional identity. A 1265 nucleotide pair cDNA encoding (1-->3)-beta-glucanase isoenzyme GII has been isolated from a library prepared with mRNA of 2-day germinated barley scutella. Nucleotide sequence analysis of the cDNA has enabled the complete primary structure of the 306 amino acid (1-->3)-beta-glucanase to be deduced, together with that of a putative NH2-terminal signal peptide of 28 amino acid residues. The (1-->3)-beta-glucanase cDNA is characterized by a high (G+C) content, which reflects a strong bias for the use of G or C in the wobble base position of codons. The amino acid sequence of the (1-->3)-beta-glucanase shows highly conserved internal domains and 52% overall positional identity with barley (1-->3, 1-->4)-beta-glucanase isoenzyme EII, an enzyme of related but quite distinct substrate specificity. Thus, the (1-->3)-beta-glucanases, which may provide a degree of protection against microbial invasion of germinated barley grain through their ability to degrade fungal cell wall polysaccharides, appear to share a common evolutionary origin with the (1-->3, 1-->4)-beta-glucanases, which function to depolymerize endosperm cell walls in the germinated grain.
Plant Mol Biol 1989 Jul
PMID:Purification of (1-->3)-beta-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone. 256 58

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

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


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