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  • 1
    Electronic Resource
    Electronic Resource
    Increased distal gene transcription by the elongation factor RfaH, a specialized homologue of NusG (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 22 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Escherichia coli RfaH protein is required for the expression of operons directing synthesis and export of the toxin haemolysin, the lipopolysaccharide core, and the F-factor sex pilus. Mutation of rfaH increases transcriptional polarity along all three operons. By demonstrating strong RfaH-dependent suppression of transcription polarity in vitro, we have established RfaH as a novel transcriptional activator, and we reveal that RfaH is a homologue of the essential protein NusG that modulates general transcriptional pausing and termination in prokaryotes. Full transcription of the distal genes from an upstream promoter required RfaH and the 5′ cis-acting ops element, both in vivo and in vitro. In vivo the requirement for the ops element was suppressed by overexpressing RfaH, and in vitro the presence of ops lowered the concentration of RfaH required to stimulate transcript elongation. We suggest that RfaH directs transcript elongation in an analogous way to NusG, but does so in a subset of bacterial operons primarily engaged in the production of extracellular components required for virulence and fertility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.d01-1726.x
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  • 2
    Electronic Resource
    Electronic Resource
    Suppression of transcription polarity in the Escherichia coli haemolysin operon by a short upstream element shared by polysaccharide and DNA transfer determinants (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 19 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Expression of the Escherichia coli hlyCABD operon encoding synthesis, maturation and export of haemolysin toxin was strongly dependent upon a 35 bp DNA sequence, spanning the element GGCGGTAG, located 2 kbp upstream. When the hly operon was placed under the control of the inducible tac promoter, expression remained dependent upon this element, when transcribed in its native orientation 3′ of the promoter. The increase in ptac-directed transcription was strongest for the distal, export genes of the hly operon, and was particularly striking when ptac and the element were placed far upstream. The element did not influence transcript stability, and we suggest that it is a key component of a novel regulatory mechanism may suppresses transcription polarity within operons. The mechanism that be of widespread importance in bacterial gene expression because the 8 bp element is present in many Gram-negative species as an upstream component of operons encoding the production of toxins and the surface assembly of polysaccharides and components required for the conjugal transfer of DNA. We name it the ops element for operon polarity suppressor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.446951.x
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  • 3
    Electronic Resource
    Electronic Resource
    A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the ‘NO releaser’, S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region (1998)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 29 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The flavohaemoglobin gene, hmp, of Escherichia coli is upregulated by nitric oxide (NO) in a SoxRS-independent manner. We now show that hmp expression is also upregulated by S-nitrosoglutathione (GSNO, widely used as an NO releaser) and sodium nitroprusside (SNP, which is a NO+ donor). Elevated homocysteine (Hcy) levels, achieved either by adding Hcy extracellularly or using metE mutants, decreased hmp expression. Conversely, metC mutants (defective in Hcy synthesis) had higher levels of hmp expression. Mutations in metR abolished hmp induction by GSNO and SNP, and hmp expression became insensitive to Hcy. We propose that the previously documented modulation by Hcy of MetR binding to the glyA-hmp intergenic regulatory region regulates hmp transcription. Although two MetR binding sites are present in this region, only the higher affinity site proximal to hmp is required for hmp induction by GSNO and SNP. GSNO and SNP react with Hcy in vitro under physiologically relevant conditions of pH and temperature generating S-nitrosohomocysteine, although in the latter case this would be co-ordinated to the Fe in SNP as a stable species. The free S-nitrosocysteine generated in the reaction with GSNO breaks down to release NO more readily than via homolysis of GSNO. As GSNO and SNP upregulate hmp similarly, the NO released in the former case on reaction with homocysteine cannot be involved in hmp regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.01000.x
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  • 4
    Electronic Resource
    Electronic Resource
    An ordered reaction mechanism for bacterial toxin acylation by the specialized acyltransferase HlyC: formation of a ternary complex with acylACP and protoxin substrates (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 34 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The 110 kDa haemolysin protoxin (proHlyA) is activated in the Escherichia coli cytosol by acyl carrier protein-dependent fatty acylation of two internal lysine residues, directed by the co-synthesized protein HlyC. Using an in vitro maturation reaction containing purified protoxin peptides and acylACP, we show unambiguously that HlyC possesses an apparently unique acyltransferase activity fully described by Michaelis–Menten analysis. The Vmax of HlyC at saturating levels of both substrates was ≈ 115 nmol acyl group min−1 mg−1 with KmacylACP of 260 nM and KmproHlyA of 27 nM, kinetic parameters sufficient to explain why in vivo HlyC is required at a concentration equimolar to proHlyA. HlyC bound the fatty acyl group from acylACP to generate an acylated HlyC intermediate that was depleted in the presence of proHlyA, but enriched in the presence of proHlyA derivatives lacking acylation target sites. HlyC was also able to bind in vivo 4′-phosphopantetheine. Substitution of conserved amino acids that could act as putative covalent attachment sites did not prevent binding of the fatty acyl or 4′-phosphopantetheine groups. These data and substrate variation analyses suggest that the unique acylation reaction does not involve covalent attachment of fatty acid to the acyltransferase, but rather that it proceeds via a sequential ordered Bi–Bi reaction mechanism, requiring the formation of a non-covalent ternary acylACP–HlyC–proHlyA complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01648.x
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  • 5
    Electronic Resource
    Electronic Resource
    Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase (1997)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 25 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A transposon (Tn10dCam) insertion mutant of Escherichia coli K-12 was isolated that exhibited hypersensitivity to zinc(II) and cadmium(II) and, to a lesser extent, cobalt(II) and nickel (II). The mutated gene, located between 75.5 and 76.2 min on the chromosome, is named zntA (for Zn(II) transport or tolerance). The metal-sensitive phenotype was complemented by a genomic DNA clone mapping at 3677.90–3684.60 kb on the physical map. Insertion of a kanamycin resistance (KnR) cassette at a Sal I site in a subcloned fragment generated a plasmid that partially complemented the zinc(II)-sensitive phenotype. DNA sequence analysis revealed that the KnR cassette was located within the putative promoter region of an ORF (o732 or yhhO) predicted to encode a protein of 732 amino acids, similar to cation transport P-type ATPases in the Cpx-type family. Inverse PCR and sequence analysis revealed that the Tn10dCam element was located within o732 in the genome of the zinc(II)-sensitive mutant. The zntA mutant had elevated amounts of intracellular and cell surface-bound Zn(II), consistent with the view that zntA+ encodes a zinc(II) efflux protein. Exposure of the zntA mutant to cobalt(II) and cadmium(II) also resulted in elevated levels of intracellular and cell surface-bound metal ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1997.mmi518.x
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  • 6
    Electronic Resource
    Electronic Resource
    A motile but non-swarming mutant of Proteus mirabilis lacks FlgN, a facilitator of flagella filament assembly (1997)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 25 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A TnphoA mutant of Proteus mirabilis was isolated, which had lost the ability to swarm, yet was still motile. The transposon had inserted into flgN, a flagella gene encoding a 147-amino-acid protein of undefined function. Proteus flgN is arranged in an operon with the class III anti-σ28 gene, flgM, flanked by the class II genes, flgA, flgBCD and flhBA, and a novel putative virulence-related gene. The flgN mutation caused a substantial reduction in cell surface-associated flagellin, particularly during differentiation to the normally hyperflagellated swarm cell. This was not due to an effect on flagella gene expression or a typical defect in the flagella export apparatus as there was no class III gene downregulation by FlgM feedback, or intracellular flagellin accumulation. Loss of FlgN nevertheless caused a severe reduction in the incorporation of pulse-labelled flagellin into the membrane/flagellum fraction of differentiating cells. Substantial amounts of both non-oligomeric flagellin and flagellin degradation products appeared in the extracellular medium, although the few mature filaments made by the mutant were no more sensitive to proteolysis than those of the wild type. FlgN appeared soluble and active in the cytosol. The data suggest that the function of FlgN is to facilitate the initiation of flagella filament assembly, a role that may be especially critical in attaining the much higher concentration of surface flagellin required for swarming. Proteus FlgN has leucine zipper-like motifs arranged on potential amphipathic helices, a feature conserved in cytosolic chaperones for the exported substrates of flagella-related type III virulence systems. While gel filtration of FlgN from the soluble cell fraction did not establish an interaction with flagellin, it indicated that FlgN may associate with an unknown component and/or form an oligomer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.5021862.x
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  • 7
    Electronic Resource
    Electronic Resource
    Role of arginine-43 and arginine-69 of the Hin recombinase catalytic domain in the binding of Hin to the hix DNA recombination sites (1997)
    Oxford UK : Blackwell Science Ltd
    Molecular microbiology 24 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Hin recombinase mediates the site-specific inversion of a segment of the Salmonella chromosome between two flanking 26 bp hix DNA recombination sites. Mutations in two amino acid residues, R43 and R69 of the catalytic domain of the Hin recombinase, were identified that can compensate for loss of binding resulting from elimination of certain major and minor groove contacts within the hix recombination sites. With one exception, the R43 and R69 mutants were also able to bind a hix sequence with an additional 4 bp added to the centre of the site, unlike wild-type Hin. Purified Hin mutants R43H and R69C had both partial cleavage and inversion activities in vitro while mutants R43L, R43C, R69S, and R69P had no detectable cleavage and inversion activities. These data support a model in which the catalytic domain plays a role in DNA-binding specificity, and suggest that the arginine residues at positions 43 and 69 function to position the Hin recombinase on the DNA for a step in the recombination reaction which occurs either at and/or prior to DNA cleavage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.4141789.x
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic differentiation among populations of Caridinazebra (Decapoda: Atyidae) in tropical rainforest streams, northern Australia (1996)
    Oxford BSL : Blackwell Science Ltd
    Freshwater biology 36 (1996), S. 0 
    Details
    ISSN: 1365-2427
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 1. Caridina zebra is a common atyid shrimp in some tropical rainforest streams in far north Queensland, Australia. Genetic variation at five allozyme loci was used to estimate the level of dispersal among populations of this species, within and between stream systems. Shrimps were sampled from nine streams in the Tully River catchment and two headwater streams in the adjacent Herbert River catchment in an area under consideration for extensive hydroelectric development.2. High levels of genetic differentiation were recorded among most populations which suggests that, like other fully aquatic species, movement is limited to a very small spatial scale.3. In the Tully catchment, populations of shrimp from streams with confluences at high altitude showed less genetic differentiation than those from streams which directly entered the lower river. Dispersal between the latter streams is clearly limited by the presence of large waterfalls and cascades.4. Adjacent stream populations were often highly differentiated, despite their close proximity, suggesting that overland dispersal is unlikely. However, populations of shrimp in the two streams in the Herbert catchment were strikingly similar in genetic structure to those in adjacent headwater streams of the Tully. Such similarity may reflect relatively recent changes in drainage patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2427.1996.00089.x
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  • 9
    Electronic Resource
    Electronic Resource
    Decision-making and diagnosis in disease management (1999)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Plant pathology 48 (1999), S. 0 
    Details
    ISSN: 1365-3059
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3059.1999.00327.x
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  • 10
    Electronic Resource
    Electronic Resource
    Efficacy of phytase on phosphorus utilization in practical diets fed to striped bass Morone saxatilis (1998)
    Oxford BSL : Blackwell Science Ltd
    Aquaculture nutrition 4 (1998), S. 0 
    Details
    ISSN: 1365-2095
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Several experiments were conducted to determine the effects of phytase on dietary phosphorus (P) utilization by striped bass Morone saxatilis fed high phytate diets. The experiments were designed to determine the effectiveness of various dietary levels of a dry or liquid phytase concentrate incorporated in diets to improve the P utilization of striped bass. Fish were fed various basal diets containing over 700 g kg−1 plant feed ingredients and 4.9–7.1 g kg−1 P and 1.5–1.7 g kg−1 non-phytin P. A diet supplemented with potassium monophosphate (PMP) and containing 9 g kg−1 total P and 6 g kg−1 non-phytin P with no added phytase was the positive control. The dietary treatments were assigned to duplicate tanks and diets were fed to juvenile striped bass for up to 14 weeks. The effectiveness of the phytase treatments was determined by measuring weight gain, feed conversion, serum, scale and vertebral calcium and P, as well as P absorption. Apparent P absorption was determined using 5 g kg−1 chromic oxide as an indigestible marker in the diet. In experiment one, significant improvements (P 〈 0.05) were found in scale and vertebral phosphorus concentrations with 2400 Phytase Units (PU) kg−1 (PU is the quantity of enzyme which liberates one micromole of inorganic P per minute from 0.015 tool L−1 sodium phytate at 37°C and pH 5.5) added to the diet. In experiment two, significant differences were observed between serum phosphorus in the phytase and no-phytase groups, while there were no differences between the positive control (PMP supplemented) and the phytase-treated fish. It was concluded that 2400 PU kg−1 of enzyme resulted in bone mineralization and serum phosphorus concentrations equal to that observed with 13 g kg−1 dietary PMP addition (9 g kg−1 total P).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2095.1998.00057.x
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