Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The arginine regulatory protein of Pseudomonas aeruginosa, ArgR, is essential for induction of operons that encode enzymes of the arginine succinyltransferase (AST) pathway, which is the primary route for arginine utilization by this organism under aerobic conditions. ArgR also induces the operon that encodes a catabolic NAD(+)-dependent glutamate dehydrogenase (GDH), which converts l-glutamate, the product of the AST pathway, in alpha-ketoglutarate. The studies reported here show that ArgR also participates in the regulation of other enzymes of glutamate metabolism. Exogenous arginine repressed the specific activities of glutamate synthase (GltBD) and anabolic NADP-dependent GDH (GdhA) in cell extracts of strain PAO1, and this repression was abolished in an argR mutant. The promoter regions of the gltBD operon, which encodes GltBD, and the gdhA gene, which encodes GdhA, were identified by primer extension experiments. Measurements of beta-galactosidase expression from gltB::lacZ and gdhA::lacZ translational fusions confirmed the role of ArgR in mediating arginine repression. Gel retardation assays demonstrated the binding of homogeneous ArgR to DNA fragments carrying the regulatory regions for the gltBD and gdhA genes. DNase I footprinting experiments showed that ArgR protects DNA sequences in the control regions for these genes that are homologous to the consensus sequence of the ArgR binding site. In silica analysis of genomic information for P. fluorescens, P. putida, and P. stutzeri suggests that the findings reported here regarding ArgR regulation of operons that encode enzymes of glutamate biosynthesis in P. aeruginosa likely apply to other pseudomonads.
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PMID:The arginine regulatory protein mediates repression by arginine of the operons encoding glutamate synthase and anabolic glutamate dehydrogenase in Pseudomonas aeruginosa. 1517 98

Potato (Solanum tuberosum L.) is highly sensitive to salt stress, which is one of the most important factors limiting plant cultivation. The investigation of plant response to high salinity was envisaged in this report using cDNA-amplified fragment length polymorphism (AFLP). This technique was applied to salt- stressed and control potato plants (cv. Nicola). The expression profiles showed approx 5000 bands. Of these, 154 were upregulated and 120 were repressed by salt stress. In this study we have only considered cDNA fragments that seem to be originated from salt-induced mRNA. Eighteen fragments were then reamplified, cloned, and sequenced. Sequence comparison of these cDNA, identified in response to salt stress in potato, revealed that some of them present homologies with proteins in other species that are involved in cell wall structure and turnover such as proline-rich proteins and beta-galactosidase. A number of identified clones encoded putative stress response proteins such as NADP-dependant glyceraldehyde dehydrogenase and wound-induced protein. In addition, some of them encode proteins related to hypersensitive response against pathogens such as putative late blight and nematode as well as putative pathogenesis-related proteins. These cDNA seem to be differentially expressed in the presence of salt stress as shown by Northern blot or reverse Northern hybridization experiments.
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PMID:Identification of salt stress-induced transcripts in potato leaves by cDNA-AFLP. 1580 74

We describe the use of a non-viral, polyethylenimine-based vector to transfect rat hepatocytes preserved under hypothermic storage. DNA sequences encoding Escherichia coli beta-galactosidase and pea ferredoxin-NADP(H) oxidoreductase (FNR), cloned into plasmids pCH110 and pKM4 respectively, were used. FNR was detected in the liver of animals transplanted with transfected cells; no reactivity was observed in endogenous parenchyma. The expression of the transgene was transient as it was detectable up to 96 h subsequently declining to undetectable levels. In contrast to non-transfected cells, the engraftment of FNR-positive cells was not associated with inflammatory reaction. The percentage of FNR-positive implanted hepatocytes was at least five times higher than the original transfection efficiency measured in vitro, while the percentage of beta-galactosidase-positive cells was similar for both methods. These data indicate that the transfection system is effective in the transfer of plasmid DNA into hepatocytes under cold preservation and suggest the advantage of pKM4-transfected hepatocytes on engraftment in the recipient parenchyma.
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PMID:Efficient cold transfection of pea ferredoxin-NADP(H) oxidoreductase into rat hepatocytes. 1628 99


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