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At least 1,513 records · Page 84Linked to original sources
PubMed1986

[Excretion of 2,3-dihydroxybenzoic acid by an enterobactin-negative multiresistant wild strain of Salmonella typhimurium].

In investigations of iron siderophores produced by different Salmonella typhimurium strains we found a strain deficient in enterobactin production. Using microbiological and chemical methods, we detected the production and excretion of 2,3-dihydrobenzoic acid, a metabolite of the enterobactin biosynthesis pathway. The strain was able to produce aerobactin. We suggest that the iron uptake of pathogenic strains can be mediated by aerobactin alone. For a correct enterobactin bioassay it is necessary to use a mutant unable to grow on 2,3-dihydroxybenzoic acid.

Chromatography, Paper↗
PubMed1972

Filamentous bacterial viruses. VII. Inhibition of fd deoxyribonucleic acid synthesis after a temperature jump into protein-synthesis inhibitors.

Synthesis of fd deoxyribonucleic acid (DNA) was stopped by transferring infected bacteria from 32 C into chloramphenicol or serine hydroxamate at 42 C, but not by addition of these antibiotics at 32 C, and not by a temperature change in the absence of antibiotics. The inhibition of fd DNA synthesis by serine hydroxamate at 42 C was reversed by excess serine. The ability to synthesize fd DNA at 42 C in chloramphenicol was rescued by delaying the addition of chloramphenicol for a few minutes after the transfer from 32 to 42 C. The colony-forming ability of abortively infected bacteria was also rescued from "killing" by delaying the addition of chloramphenicol after a transfer from 32 to 42 C.

Centrifugation, Density Gradient↗
PubMed1996

Expression and distribution of meprin protease subunits in mouse intestine.

Meprins, zinc metalloendopeptidases of kidney and intestinal brush border membranes, are composed of differing ratios of alpha and beta subunits. Previous work indicated that the beta subunit was expressed in kidney and intestine of all mouse strains, but that the alpha subunit was only expressed in kidney of random-bred and some inbred strains and not in mouse intestine. The work herein, however, reports that low levels of meprin alpha subunit mRNA and protein are detectable in mouse intestine and are present in increasing concentrations from the duodenum to the ileum. In ICR mice, the duodenum expressed less than 1% of the meprin alpha mRNA (micrograms/g tissue) relative to kidney, the ileum approximately 20%. The large intestine contained approximately 10% of the message found in kidney. An inbred mouse strain, C3H/He, found previously to contain only meprin beta subunits in kidney and intestine, displayed very low levels of meprin alpha mRNA (approximately 1% of that in ICR kidney) in both the kidney and intestine. Intestinal meprin beta mRNA in ICR and C3H/He mice, by contrast, was expressed at similar levels to that found in kidney, and for both strains there was an increase (two- to threefold) in the beta message in the ileum relative to duodenum or jejunum. In general, the pattern of the meprin alpha protein along the intestine was similar to that of alpha mRNA, and activity and response of intestinal meprin A to inhibitors were typical of the enzyme isolated from kidney. These data indicate that meprin alpha can be detected in mouse small and large intestine and that expression is not only tissue- and strain-specific but also longitudinally variable in intestine. The expression pattern for both a and beta subunits indicates an ileal function for the meprins.

Amino Acid Sequence↗
PubMed1994

Histone acetylation influences both gene expression and development of Xenopus laevis.

We examine the potential role of histone hyperacetylation in gene activation during Xenopus development using Trichostatin A, (TSA), a specific inhibitor of histone deacetylase. We find that TSA is very effective in inducing both core histone hyperacetylation and histone H1(0) gene expression in a Xenopus somatic cell line. In contrast, TSA does not induce histone hyperacetylation or histone H1(0) transcription in Xenopus oocytes. Histone hyperacetylation is developmentally regulated during Xenopus embryogenesis; hyperacetylated histones first accumulate early in gastrulation. The capacity of TSA to induce histone H1(0) gene expression correlates with the induction of histone hyperacetylation. Concentrations of TSA sufficient to induce histone hyperacetylation in Xenopus embryos delay gastrulation and cause diminished midtrunk and posterior formation, suggesting defects in mesoderm formation. Although the constitutive hyperacetylation of the histones does not prevent either the cell division or differentiation sufficient for early morphogenesis it has a role in establishing stable states of differential gene activity during gastrulation.

Acetylation↗
PubMed1995

Purification and properties of urease from Sporobolomyces roseus.

Urease (EC 3.5.1.5) catalyses the hydrolysis of urea to ammonia and carbon dioxide. The enzyme from Sporobolomyces roseus was enriched 780-fold and purified to apparent homogeneity using heat treatment, ion exchange chromatography on Q-Sepharose fast flow, hydrophobic interaction chromatography on Phenyl-Sepharose, size exclusion chromatography on Sephacryl S 300 HR, and ion exchange chromatography on MonoQ. Analysis of the purified enzyme by SDS-PAGE demonstrated the presence of subunits with a molecular weight of 90 (+/- 4) kDa. The M(r) of the native enzyme was estimated by size exclusion chromatography to be 340 (+/- 30) kDa, suggesting a tetrameric structure different from other ureases isolated so far from both prokaryotes and eukaryotes. The enzyme was heat-stable, showing no loss of activity after incubation at 70 degrees C for 15 min. The highest urease activities were observed after growth on media containing urea as the sole source of nitrogen.

Chelating Agents↗
PubMed2003

TSC2 regulates VEGF through mTOR-dependent and -independent pathways.

Inactivation of the TSC2 tumor suppressor protein causes tuberous sclerosis complex (TSC), a disease characterized by highly vascular tumors. TSC2 has multiple functions including inhibition of mTOR (mammalian target of Rapamycin). We found that TSC2 regulates VEGF through mTOR-dependent and -independent pathways. TSC2 loss results in the accumulation of HIF-1alpha and increased expression of HIF-responsive genes including VEGF. Wild-type TSC2, but not a disease-associated TSC2 mutant, downregulates HIF. Rapamycin normalizes HIF levels in TSC2(-/-) cells, indicating that TSC2 regulates HIF by inhibiting mTOR. In contrast, Rapamycin only partially downregulates VEGF in this setting, implying an mTOR-independent link between TSC2 loss and VEGF. This pathway may involve chromatin remodeling since the HDAC inhibitor Trichostatin A downregulates VEGF in TSC2(-/-) cells.

Animals↗