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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
    Novel shuttle vectors for improved streptokinase expression in streptococci and bacterial L-forms (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 65 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Novel shuttle vectors of small size and increased copy number capable of replication in Escherichia coli, L-forms of Proteus miabilis, and streptococci were constructed from a streptococcal erythromycin-resistant plasmid and an Escherichia coli phasmid. The streptokinase gene, skc, was inserted into one of them, and skc expression was studied in Streptococcus sanguis, Streptococcus lactis, and in an L-form strain (LVI) of Proteus mirabilis. The new streptokinase shuttle plasmid, pMLS10 (7.3 kb), specified higher Skc yields in all hosts when compared to pSM752 constructed previously. In particular Proteus mirabilis LVI(pMLS10) proved to be the most productive host, exhibiting complete secretion of the active protein at yields as high as 24 000 unit per ml.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03602.x
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  • 3
    Electronic Resource
    Electronic Resource
    Heterologous signal peptide processing in fusion interferon synthesis by engineered L-forms of Proteus mirabilis (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 59 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A recombinant DNA Proteus mirabilis L-form expression system, LVI (pJS127), was used to synthesize human fusion interferon alpha 1 (f-IFN-α1). In the expression plasmid used, the complete coding sequence of IFN-α1 was linked to the streptococcal speA promoter and the 5′ end of the speA structural gene including its signal sequence coding region. LVI (pJS127) was capable of complete secretion into the culture medium of biologically active f-IFN-α1 whose identity was confirmed by immunological and chemical evidence. In particular, bacterial L-forms were for the first time shown to be capable of correct signal peptide processing, as determined by N-terminal sequencing of the secreted f-IFN.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03083.x
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  • 4
    Electronic Resource
    Electronic Resource
    Electron microscopic analysis of protoplast fusion in Streptomyces hygroscopicus and consideration on structural alterations in fusing membranes (1980)
    Springer
    Archives of microbiology 126 (1980), S. 263-269 
    Details
    ISSN: 1432-072X
    Keywords: Ultrastructural analysis ; Protoplast fusion ; Fusion products ; Membrane fusion ; Streptomyces hygroscopicus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protoplasts of Streptomyces hygroscopicus were treated with polyethylene glycol and prepared for electron microscopic investigation as ultrathin sections. About 5% binary fusion products and 0.9% multicellular fusion products have been obtained in the sections. Three main types may be differentiated among binary fusion products, characterized by a successive loss of the bispherical shape and of continuous membrane structures in fusion zones. Analysing the membrane alterations a contact zone characterized by intact cytoplasmic membranes in both protoplasts, a fusion zone with a trilaminar fusion membrane of about 13–17 nm in thickness, and a fusion zone without continuous membrane structure can be distinguished. The different fusion areas are considered as stages in the fusion process. The data will be discussed in conjunction with a model for membrane alterations during fusion at the molecular level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409930
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  • 5
    Electronic Resource
    Electronic Resource
    The Serratia marcescens hemolysin is secreted but not activated by stable protoplast-type L-forms of Proteus mirabilis (1998)
    Springer
    Archives of microbiology 170 (1998), S. 236-242 
    Details
    ISSN: 1432-072X
    Keywords: Key words Hemolysin ; Activation ; Secretion ; L-forms ; Protoplasts ; Serratia marcescens ; Proteus mirabilis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The outer-membrane protein ShlB of Serratia marcescens activates and secretes hemolytic ShlA into the culture medium. Without ShlB, inactive ShlA (termed ShlA*) remains in the periplasm. Since Proteus mirabilis L-form cells lack an outer membrane and a periplasm, it was of interest to determine in which compartment recombinant ShlA* and ShlB are localized and whether ShlB activates ShlA*. The cloned shlB and shlA genes were transcribed in P. mirabilis stable L-form cells by the temperature-inducible phage T7 RNA polymerase. Radiolabeling, Western blotting, and complementation with C-terminally truncated ShlA (ShlA255) identified inactive ShlA* in the culture supernatant. ShlB remained cell-bound and did not activate ShlA without integration in an outer membrane. Although hemolytic ShlA added to L-form cells had access to the cytoplasmic membrane, it did not affect L-form cells. Synthesis of the large ShlA protein (165 kDa) in P. mirabilis L-form cells under phage T7 promoter control demonstrates that L-form cells are suitable for the synthesis and secretion of large recombinant proteins. This property and the easy isolation of released proteins make L-form cells suitable for the biotechnological production of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050638
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