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  • 1
    Electronic Resource
    Electronic Resource
    Molecular characterization of hpuAB, the haemoglobin–haptoglobin-utilization operon of Neisseria meningitidis (1997)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 23 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We previously identified HpuB, an 85 kDa Fe-repressible protein required for utilization of Fe from, and binding to, haemoglobin and the haemoglobin–haptoglobin complex. The gene for hpuB was cloned from Neisseria meningitidis strain DNM2 and the predicted amino acid sequence indicates that HpuB is an outer membrane receptor belonging to the TonB family of high-affinity transport proteins. A second open reading frame, predicted to encode a 34.8 kDa lipoprotein, was discovered 5′ to hpuB, and was designated hpuA. HpuA was identified in a total-membrane-protein preparation by construction of a mutant lacking HpuA. Acylation of HpuA was confirmed by [3H]-palmitic acid labelling of meningococci. Consensus promoter sequences were not apparent 5′ to hpuB. The hpuA insertion mutation exerted a polar effect, abolishing expression of hpuB, suggesting that hpuA and hpuB are co-transcribed. The 3.5 kb polycistronic hpuAB mRNA was identified and shown to be transcriptionally repressed by iron. The transcriptional start site was identified 33 nucleotides 5′ to the hpuA translational start site, appropriately positioned around consensus promoter and ferric uptake regulator (Fur)-box sequences. The structure of this operon suggests that HpuA–HpuB is a two-component receptor analogous to the bipartite transferrin receptor TbpB–TbpA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.2501619.x
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  • 2
    Electronic Resource
    Electronic Resource
    Parameter estimation in surface exchange models using nonlinear inversion: how many parameters can we estimate and which measurements are most useful? (2001)
    Oxford, UK : Blackwell Science Ltd
    Global change biology 7 (2001), S. 0 
    Details
    ISSN: 1365-2486
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Geography
    Notes: Models of mass and energy exchanges between the biosphere and the atmosphere generally contain a nonlinear dependence between fluxes and model parameters, and thus estimation of these parameters from measurements in a heterogeneous landscape depends on the scale of the observations. The scale-dependence of a typical surface-exchange model (the CSIRO Biospheric Model, CBM) is examined using the diurnal variation of hourly fluxes of CO2, latent heat, sensible heat and soil heat. The fluxes were measured using micrometeorological techniques over six sites in a grazing/pasture system in SE Australia during a period of three weeks in 1995. Nonlinear parameter inversion was used to determine model parameters.Analysis of the covariance of the estimates of the parameters and the unexplained residuals of the model showed that a maximum of three or four parameters could be determined independently from the observations for all six sites. Estimates of a key model parameter, jmax, the mean of maximum potential electron transport rate of all leaves within the canopy, was best determined by the measurements of net CO2 flux at all sites examined. Measurements of ground heat flux provide little information about any of the model parameters in CBM.Because of nonlinearities in the surface exchange model, calculated fluxes will be in error if parameters for the component vegetation types are simply averaged in proportion to their areal fraction. The magnitude of these errors was examined for CBM using a hypothetical land surface consisting of two surface types, each with different parameter values. Predictions of net CO2, latent heat and ground heat fluxes using a linear combination of model parameters for the two surface types were quite similar with those found using optimal estimates of the parameters for the landscape, but were significantly poorer for sensible heat fluxes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2486.2001.00434.x
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  • 3
    Electronic Resource
    Electronic Resource
    A conserved region in the σ54-dependent activator DctD is involved in both binding to RNA polymerase and coupling ATP hydrolysis to activation (1997)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 26 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Rhizobium melioti DctD activates transcription from the dctA promoter by catalysing the isomerization of closed complexes between σ54-RNA polymerase holoenzyme and the promoter to open complexes. DctD must make productive contact with σ54-holoenzyme and hydrolyse ATP to catalyse this isomerization. To define further the activation process, we sought to isolate mutants of DctD that had reduced affinities for σ54-holoenzyme. Mutagenesis was confined to the well-conserved C3 region of the protein, which is required for coupling ATP hydrolysis to open complex formation in σ54-dependent activators. Mutant forms of DctD that failed to activate transcription and had substitutions in the C-terminal half of the C3 region were efficiently cross-linked to σ54 and the β-subunit of RNA polymerase, suggesting that they bound normally to σ54-holoenzyme. In contrast, some mutant forms of DctD with amino acid substitutions in the N-terminal half of the C3 region had reduced affinities for σ54 and the β-subunit in the cross-linking assay. These data suggest that the N-terminal half of the C3 region of DctD contains a site that may contact σ54-holoenzyme during open complex formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.5851955.x
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