Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The PRB-1b gene codes for a basic-type pathogenesis-related protein of the PR-1 family of tobacco. PRB-1b mRNA accumulation is induced in response to biotic and abiotic elicitors, such as TMV, ethylene, salicylic acid, alpha-amino butyric acid and darkness. In order to determine the location of elements that control dark-regulated PRB-1b gene expression, we tested promoter, transcribed regions and 3'-downstream regions of the gene for their ability to respond to dark induction in transgenic tobacco plants. An ethylene-inducible promoter region of 863 bp was not able to confer dark induction to a beta-glucuronidase reporter gene, while a construct containing the transcribed region of the gene and 3'-downstream sequences, driven by the cauliflower mosaic virus 35S promoter, was correctly dark-regulated. The results indicate that dark-induction of the PRB-1b gene can be controlled by 3'-downstream elements at the transcriptional level or by transcribed sequences at the post-transcriptional level. A circadian clock regulation of the PRB-1b gene was excluded, as fluctuations of PRB-1b transcript levels were not observed in plants placed in constant light or darkness. Subcellular localization of the PRB-1b protein was also determined, in tobacco protoplasts preparations and in cell cultures. The PRB-1b polypeptide was predominantly detected in protoplast vacuoles and was not secreted to the media in cell cultures. These results support an intracellular localization for the PRB-1b protein, as reported for other basic-type components of the pathogenesis-related proteins family.
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PMID:Dark induction and subcellular localization of the pathogenesis-related PRB-1b protein. 763 22

A number of A/T-rich sequences and a CATGCAT/A sequence are contained in the 5'-upstream regions of the genes encoding concanavalin A (Con A) and canavalin, two major seed storage proteins of Canavalia gladiata D.C. To study the role of these sequences in the seed-specific gene expression, we constructed 5'-deletion mutants and examined the transient expression of beta-glucuronidase reporter gene by particle bombardment and the stable expression by Agrobacterium-mediated transformation of tobacco plants. Positive regulatory elements were located in the -894/-602 and -602/-74 regions of the Con A gene, and in the -428/-376, -281/-155 and -155/-50 regions of the canavalin gene. In addition, the results suggested that the A/T-rich sequences in the 5'-upstream region of the Con A gene play a role in transcriptional activation, but that those of the canavalin gene have little effect on the gene expression. The CATGCAT/A sequence was not sufficient by itself for high levels of expression of both the Con A and canavalin genes. The canavalin polypeptide amounted to about 1% of the total extractable protein in the transgenic tobacco seeds, but the Con A polypeptide was not detected in the extractable protein.
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PMID:Promoter analysis of seed storage protein genes from Canavalia gladiata D.C. 772 50

Appressorium formation in germinating Colletotrichum gloeosporioides is induced by the surface wax of the host, the avocado fruit. To elucidate the mechanism by which differentiation of appressorium formation is induced, the fungal genes specifically activated by this host signal were sought. From a cDNA library of the transcripts present in appressorium-forming conidia, the clones representing nongerminating conidia were removed by hybridization with cDNAs synthesized from the nongerminating conidia. From this subtracted library, clones that hybridized with cDNA for transcripts from appressorium-forming conidia and not with cDNA for transcripts from germinating conidia were selected. Three such clones were isolated and sequenced. The genes for these three transcripts were also cloned and sequenced. Northern blot analysis showed that transcripts that hybridized with these three clones were expressed in the conidium only during the process of appressorium formation induced by avocado surface wax, and that these transcripts were not detectable when appressorium formation was prevented even in the presence of avocado wax. Nucleotide sequences of the clones revealed that one clone, cap3, contained an open reading frame (ORF) that would code for a 26-amino acid, cysteine-rich peptide with significant homology to Neurospora crassa copper metallothionein. Another clone, cap5, contained an ORF that would code for a 27-amino acid cysteine-rich peptide with less homology to metallothioneins. Cu2+ and Cd2+ also induced the expression of these genes at lower levels. The histochemical analysis of transformants containing the cap5 promoter fused to the beta-glucuronidase (GUS) gene showed that the cap5 gene promoter caused GUS expression exclusively during appressorium formation and most of the gus activity was in the appressorium. The cap22 clone contained an ORF coding for a 227-amino acid polypeptide of 22 kDa, which did not show significant homology to any known proteins. Recombinant CAP22 protein was produced using a pET-19b expression system in Escherichia coli, purified, and used to prepare rabbit antibodies. Western blot analysis of proteins from the appressorium-forming conidia revealed a major cross-reacting protein at 43 kDa and a minor band at 68 kDa, indicating that the potential glycosylation sites found in the primary translation product were probably glycosylated. Results of immunogold localization showed that CAP22 protein was located on the wall of the appressorium.
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PMID:Isolation and characterization of genes expressed uniquely during appressorium formation by Colletotrichum gloeosporioides conidia induced by the host surface wax. 777 33

A genomic clone encoding the gamma-kafirin gene from sorghum was isolated and sequenced. A 2938 bp sequenced fragment includes an intronless open reading frame of 636 nucleotides encoding a putative polypeptide of 212 amino acids. Comparison of the deduced amino acid sequence of gamma-kafirin with the published sequences of gamma-prolamins of maize, and Coix revealed highly conserved domains. The N-terminal region of these proteins contains the conserved hexapeptide PPPVHL, which is repeated eight times in gamma-zein, four times in gamma-kafirin and three times in gamma-coixin. The number of PPPVHL repeats accounts predominantly for the differences in the molecular weights of gamma-prolamins. Several putative regulatory sequences common to the gamma-kafirin and gamma-zein genes were identified in both the 5' and the 3' flanking regions. Putative GCN4-like regulatory sequences were found at positions -192 and -476 in the 5' flanking region of gamma-kafirin. In the 3' noncoding region, three putative polyadenylation signals, two AATAAT and one AATGAA, were found at positions +658, +716, and +785, respectively. In order to investigate the role of the putative GCN4-like motifs and other possible cis-acting element(s) of the gamma-kafirin promoter, a series of deleted and chimeric promoter constructs were introduced into maize, Coix and sorghum tissues by particle bombardment. Histochemical analysis of beta-glucuronidase (GUS) activity in different tissues indicated that the element(s) responsible for tissue specificity is probably located in the 285-bp proximal region of the promoter, while the remaining promoter sequence seems to carry the element(s) responsible for the quantitative response.
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PMID:Structural characterization and promoter activity analysis of the gamma-kafirin gene from sorghum. 781 25

Two cDNA clones (RCc2 and RCc3) corresponding to mRNAs highly expressed only in root tissues of rice (Oryza sativa L.) seedlings were characterized. Respectively, they encode polypeptides of 146 (14.5 kDa) and 133 amino acids (13.4 kDa) that share high (> 70%) sequence similarity with a polypeptide encoded by a cDNA (ZRP3) encoding an mRNA preferentially expressed in young maize roots. Genomic DNA blot analysis revealed that they are members of a small gene family and RCg2, the gene corresponding to RCc2, was isolated. A 1656 bp 5'-upstream sequence of RCg2 was translationally fused to a beta-glucuronidase (GUS) reporter gene and stable introduction of the chimeric construct into rice was confirmed by PCR and genomic DNA blot analyses. Histochemical analysis of transgenic rice plants containing the full-length chimeric gene showed high levels of GUS activity in mature cells and the elongation and maturation zones of primary and secondary roots, and in the root caps, but no GUS activity was detected in root meristematic regions. Surprisingly, high GUS activity was also detected in leaves of the same plants. This raises the possibility that the RCg2 5'-upstream element may not be sufficient for the proper spatial control of root specificity in transgenic rice.
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PMID:Characterization of a rice gene family encoding root-specific proteins. 788 15

A genomic clone encoding the precursor of wheat leaf ferredoxin has been isolated and characterised. The uninterrupted PetF gene encodes a polypeptide of 143 amino acid residues, consisting of an N-terminal presequence of 46 amino acid residues and a mature polypeptide of 97 amino acid residues. Southern blot analysis suggests that six copies of the PetF gene are present in the wheat haploid genome. Northern blot analysis has shown that the genes are both developmentally and light regulated in wheat seedlings and provides evidence that a circadian rhythm regulates the steady-state levels of ferredoxin transcripts. The intact wheat gene and several chimeric constructs, containing portions of the 5'-upstream region fused to the beta-glucuronidase reporter gene, have been introduced into tobacco plants, but levels of beta-glucuronidase activity above background were not detected, suggesting that the 5'-upstream region is unable to function as a promoter in tobacco plants.
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PMID:Developmental, circadian and light regulation of wheat ferredoxin gene expression. 788 19

Two protein kinase genes (atpk1 and atpk2) were isolated from Arabidopsis thaliana genomic DNA with a probe generated by polymerase chain reaction (PCR) using oligonucleotide primers encoding conserved eukaryotic protein kinase sequences. atpk1 and atpk2 are organized in a head-to-tail tandem array on chromosome 3 and have about 80% nucleotide sequence identity. atpk1 encodes a hydrophilic polypeptide of 465 amino acids, M(r) = 52,554. The centrally located catalytic domain contains all the conserved residues characteristic of eukaryotic protein kinases, with greatest similarity to the catalytic domains of 70-kDa ribosomal S6 protein kinase, protein kinase C, and protein kinase A. The C-terminal 75 residues also show homology to protein kinase C and S6 protein kinase. In contrast, the N-terminal 130 residues have no homology to any known protein, and thus may represent a new class of protein kinase regulatory domain. Other motifs found in the Atpk1 protein include two putative autophosphorylation sites, a pseudosubstrate site, two acidic domains, a lysine-rich domain, and two putative PEST sequences, which may contribute to the regulation of protein kinase activity. RNA-blot hybridization showed that atpk1 encoded a 1.8-kb mRNA. Analysis of atpk1 promoter/beta-glucuronidase reporter gene fusions in transgenic plants showed that atpk1 was expressed in all tissues and at all developmental stages, with the strongest expression observed in metabolically active tissues, suggesting that atpk1 is involved in the control of plant growth and development. The first intron of atpk1 functions as an enhancer in atpk1 expression.
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PMID:atpk1, a novel ribosomal protein kinase gene from Arabidopsis. I. Isolation, characterization, and expression. 791 97

The neutrophil plasma membrane has a major role in migration, phagocytosis, and destruction of microorganisms. Neutrophils isolated from blood and mammary secretions were homogenized, and the plasma membrane fraction was isolated on discontinuous sucrose gradient (20, 32, and 50%). Purity of plasma membrane preparation was determined by use of marker enzyme analysis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the membrane proteins was performed under reducing conditions for polypeptide characterization. The membrane proteins were also labeled with 125I externally, using 1,3,4,6-tetrachloro-3 alpha-6 alpha-diphenylglycouril, and proteins were separated by SDS-PAGE and autoradiographed. Compared with whole cell homogenate, the plasma membrane fraction obtained at the 20/32% interface was enriched for the marker enzymes, 5'-nucleotidase (16-fold), alkaline phosphatase (5.5-fold), and total phosphatase (26-fold). The membrane fraction had minimal specific activity for beta-glucuronidase (0.4-fold), compared with whole cell homogenate. Plasma membrane protein yield was about 500 micrograms/10(9) bovine blood neutrophils. The SDS-PAGE of plasma membrane proteins revealed 25 protein bands, of which 13 were major bands. There were 3 distinct bands (18, 36, and 65 kd) in the plasma membrane-enriched fraction (20/32 interface) that were not seen in other fractions (30/50% and pellet). Further, 125I-labeling identified 5 distinct protein bands (205, 140, 65, 35, and 30 kd). Blood and mammary neutrophils had similar polypeptide patterns, except that 36- and 65-kd bands were more prominent for blood neutrophils than for mammary neutrophils.
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PMID:Isolation and partial polypeptide characterization of bovine neutrophil plasma membranes. 794 18

The plastid psbA gene encodes the 32 kDa D1 polypeptide of photosystem II. It has previously been shown that the initiation of psbA mRNA translation in tobacco is regulated by sequences outside of the coding region. To identify the cis-acting regulatory sequences involved in the translational control, a series of chimeric uidA genes, encoding the beta-glucuronidase (GUS) reporter enzyme, were introduced into the plastid genome. GUS accumulation in response to the light (135- to 200-fold), and the arrest of uidA mRNA translation in light-grown seedlings following transfer for 2 h to the dark, was observed only if the transgenes contained the psbA 5'-untranslated leader region (UTR). Changes in GUS accumulation were accompanied by little or no changes in the uidA mRNA levels. The data indicate that the initiation of D1 translation in tobacco plastids is controlled via the psbA 5'-UTR.
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PMID:Translation of psbA mRNA is regulated by light via the 5'-untranslated region in tobacco plastids. 798 13

A 5-kDa polypeptide, pseudothionin Solanum tuberosum 1 (Pth-St1), which was active against Clavibacter michiganensis subspecies sepedonicus, a bacterial pathogen of potatoes, has been purified from the buffer-insoluble fraction of potato tubers by salt extraction and HPCL. Pth-St1 was also active against other potato pathogens tested (Pseudomonas solanacearum and Fusarium solani). The N-terminal amino acid sequence of this peptide was identical (except for a N/H substitution at position 2) to that deduced from a previously reported cDNA sequence (EMBL accession number X-13180), which had been misclassified as a Browman-Birk protease inhibitor. Pth-St1 did not inhibit either trypsin or insect alpha-amylase activities, and, in contrast with true thionins, did not affect cell-free protein synthesis or beta-glucuronidase activity. Northern-blot and tissue-print analyses showed that steady-state mRNA levels were highest in flowers (especially in petals), followed by tubers (especially in the epidermal cell layers and in leaf primordia), stems and leaves. Infection of leaves with a bacterial pathogen suspended in 10 mM MgCl2 switched off the gene, whereas mock inoculation with 10 mM MgCl2 alone induced higher mRNA levels.
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PMID:Pseudothionin-St1, a potato peptide active against potato pathogens. 803 86


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