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  • Blackwell Publishing Ltd  (3)
Document type
Publisher
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  • 1
    Electronic Resource
    Electronic Resource
    Signal transduction in bacteria: phospho-neural network(s) in Escherichia coli? (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 16 (1995), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: The molecular basis of many forms of signal transfer in living organisms is provided via the transient phosphorylation of regulatory proteins by transfer of phosphoryl groups between these proteins. The dominant form of signal transduction in prokaryotic microorganisms proceeds via so-called two-component regulatory systems. These systems constitute phosphoryl transfer pathways, consisting of two or more components. Most of these pathways are linear, but some converge and some are divergent. The molecular properties of some of the well-characterised representatives of two-component systems comply with the requirements to be put upon the elements of a neural network: they function as logical operators and show the phenomenon of autoamplification. Because there are many phosphoryl transfer pathways in parallel and because there also appears to be cross-talk between these pathways, the total of all two-component regulatory systems in a single prokaryotic cell may show the typical characteristics fo a ‘phospho-neural network’. This may wel lead to signal amplification, associative responses and memory effects, characteristics which are typical for neural networks. One of the main challenges in molecular microbial physiology is to determine the extent of the connectivity of the constituting elements of this presumed ‘phospho-neural network’, and to outline the extent of intelligence-like behaviour this network can generate. Escherichia coli is the organism of choice for this characterization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1995.tb00178.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of a ptsH homologue from Streptomyces coelicolor A3(2) (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 177 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A ptsH homologue of Streptomyces coelicolor A3(2) was identified in the emerging genome sequence, cloned in Escherichia coli and the S. coelicolor HPr over-produced and purified. The protein was phosphorylated in vitro in a phosphoenolpyruvate (PEP)-dependent manner by purified enzyme I (EI) from Bacillus subtilis, and much less efficiently in an ATP-dependent manner by purified HPr kinase, also from B. subtilis. There was no indication of ATP-dependent phosphorylation of the purified protein by cell extracts of either S. coelicolor or Streptomyces lividans. Deletion of the ptsH homologue from the S. coelicolor and S. lividans chromosomes had no effect on growth when fructose was supplied as sole carbon source, and in S. coelicolor it had no effect on glucose repression of agarase and galactokinase synthesis, suggesting that the HPr encoded by this gene does not play an essential role in fructose transport nor a general role in carbon catabolite repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13744.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Non-physiological expression of UhpT does not lead to uncontrolled leakage of sugar phosphates out of Escherichia coli cells (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 131 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract De-regulated expression of uhpT under control of the tac promoter, by increasing concentrations of isopropyl-thio-β-d-galactoside, progressively inhibited the growth rate of Escherichia coli cells, to such an extent that growth was fully inhibited at 1 mM of the inducer. Significantly, addition of glucose 6-phosphate to the growth medium of the cells did not protect against this inhibition. Furthermore, efflux of sugar phosphates from the cells did not take place under these conditions, unless protonophoric uncouplers were added. We therefore conclude that the regulation of uhpT expression i.e. via extracellular induction through a two-component system, did not evolve in order to prevent loss of essential metabolites from the cytoplasm under conditions when extracellular sugar phosphates are not available.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07748.x
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    Paper (German National Licenses)
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