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  • 1
    Electronic Resource
    Electronic Resource
    Introduction of a mini-gene encoding a five-amino acid peptide confers erythromycin resistance on Bacillus subtilis and provides temporary erythromycin protection in Proteus mirabilis (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 182 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A 15-bp mini-gene was introduced into Bacillus subtilis and into stable protoplast-like L-forms of Proteus mirabilis. This mini-gene encoded the peptide MVLFV and modeled a fragment of Escherichia coli 23S rRNA responsible for E. coli erythromycin (Ery) resistance. Expression of the introduced mini-gene conferred permanent Ery resistance on B. subtilis. In L-forms of P. mirabilis, the Ery-protective effect was maintained in the course of several generations. Herewith, the mechanism of Ery resistance mediated by expression of specific short peptides was shown to exist in evolutionary distant bacteria. Three new plasmids were constructed containing the gene under study transcriptionally fused with the genes encoding glutamylendopeptidase of Bacillus licheniformis or δ-endotoxin of Bacillus thuringiensis. The Ery resistance pentapeptide (E-peptide) mini-gene served as an efficient direct transcriptional reporter and allowed to select bacillar glutamylendopeptidase with improved productivity. The mini-genes encoding E-peptides may be applied as selective markers to transform both Gram-positive and Gram-negative bacteria. The small size of the E-peptide mini-genes makes them attractive selective markers for vector construction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb08897.x
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  • 2
    Electronic Resource
    Electronic Resource
    A novel protein kinase that controls carbon catabolite repression in bacteria (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: HPr(Ser) kinase is the sensor in a multicomponent phosphorelay system that controls catabolite repression, sugar transport and carbon metabolism in Gram-positive bacteria. Unlike most other protein kinases, it recognizes the tertiary structure in its target protein, HPr, a phosphocarrier protein of the bacterial phosphotransferase system and a transcriptional cofactor controlling the phenomenon of catabolite repression. We have identified the gene (ptsK) encoding this serine/threonine protein kinase and characterized the purified protein product. Orthologues of PtsK have been identified only in bacteria. These proteins constitute a novel family unrelated to other previously characterized protein phosphorylating enzymes. The Bacillus subtilis kinase is shown to be allosterically activated by metabolites such as fructose 1,6-bisphosphate and inhibited by inorganic phosphate. In contrast to wild-type B. subtilis, the ptsK mutant is insensitive to transcriptional regulation by catabolite repression. The reported results advance our understanding of phosphorylation-dependent carbon control mechanisms in Gram-positive bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00747.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Evidence for an efflux carrier system involved in the secretion of glutamate by Corynebacterium glutamicum (1989)
    Springer
    Archives of microbiology 151 (1989), S. 342-347 
    Details
    ISSN: 1432-072X
    Keywords: Amino acid ; Carrier ; Corynebacterium glutamicum ; Efflux ; Glutamate ; Kinetics ; Membrane ; Secretion ; Transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Corynebacterium glutamicum effectively secretes L-glutamate when growing under biotin limitation. The secretion of glutamate was studied with respect to kinetic and energetic parameters: rate of glutamate uptake and efflux, specificity of transport, dependence of efflux on the energy state of the cell, concentration gradient of glutamate and ions, and membrane potential. By comparing these parameters when measured in biotin-limited, i.e. “producer” cells, and biotin-supplemented, i.e. “non-producer” cells, respectively, the following conclusions could be drawn: 1. The efflux of L-glutamate in C. glutamicum cannot be explained by passive permeation of this amino acid through the plasma membrane, as it has been assumed in the generally accepted model of glutamate secretion in biotin-limited cells. 2. It is unlikely that the efflux of glutamate occurs via an inversion of the glutamate uptake system. 3. Based on our results concerning the specificity and the kinetics of glutamate transport as well as the observed regulation phenomena, we conclude that secretion of glutamate in C. glutamicum occurs by a special efflux carrier system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406562
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