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  • 1
    Electronic Resource
    Electronic Resource
    Preferential synthesis, localisation and solubilisation of a precursor form of Bacillus subtilis levansucrase in an Escherichia coli minicell system (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 30 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract In the presence of phenethylalcohol, plasmidencoded levansucrase (2,6β-d-fructan: 6,β-d-fructosyltransferase, EC 2.4.1.10) was accumulated as a precursor form in the membrane fraction of Escherichia coli minicells. Immunoblotting experiments were used to evaluate the amount of the newly synthesised precursor form relative to the immunoreactivity of the purified mature form of levansucrase. Solubilisation of both forms with Triton X100 and Triton X114 was compared. Triton X114 allowed separation of the precursor form from the mature form, which were recovered in the detergent and the aqueous phases, respectively, after separation of the phases at 30°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb01003.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Bacillus subtilisα-amylase: the rate limiting step of secretion is growth phase-independent (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 173 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: When Bacillus subtilisα-amylase was expressed under the control of sacR in a degU32(Hy) strain, the production of exoenzyme occurred during both the exponential and stationary phases of growth. In each phase, pulse-chase experiments showed that the rate-limiting step of the secretion process was the release of the processed form of the protein in each physiological context. The rate of this event was slightly slower (t1/2=3.2 min) during the stationary phase than during the exponential phase (t1/2=2 min). The effectors which possibly control the efficiency of the release stage, the level of PrsA or the calcium binding properties of the cell wall, remained unchanged throughout growth phases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13493.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 9 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A weak Ca2+-binding site (Ka= 0.8× 103 M−1, at pH7) was identified in the mature part of levansucrase. An amino acid substitution (Thr-236 →lle) in this site alters simultaneously the affinity for calcium, the folding transition and the efficiency of the secretion process of levansucrase. Moreover, the ability of the Bacillus subtilis cell wall to concentrate calcium ions present in the culture medium was studied. We confirm the results of Beveridge and Murray who showed that the concentration factor is about 100 to 120 times. This property preserves a high concentration of Ca2+ (〉2 mM) on the external side of the cytoplasmic membrane, even in the absence of further Ca2+ supplementation in the growth medium. Such local conditions allow the spontaneous unfolding folding transition of levansucrase en route for secretion. Since several exocellular proteins of B. subtilis are calcium-binding proteins, we propose that the high concentration of calcium ion in the microenvironment of the cell wall may play a key role in the ultimate step of their secretion process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01239.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Extracellular levansucrase of Bacillus subtilis produced in yeast remains in the cell in its precursor form (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 29-38 
    Details
    ISSN: 0749-503X
    Keywords: Heterologous gene expression ; levansucrase precursor ; Bacillus subtilis ; yeast ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Levansucrase, a Bacillus subtilis extracellular enzyme, was not secreted in the culture medium when produced in yeast. The protein accumulated inside the cell in its precursor form which represented 0·3% of total proteins. The absence of any post-translational modifications, such as signal sequence cleavage or addition of N-linked sugars, indicated that this protein did not enter the reticulum secretion pathway.Direct observation of the cells by confocal laser scanning microscopy showed that levansucrase was associated with the cytoplasmic membrane. Subcellular fractionation experiments revealed that levansucrase precursor form is associated with membranes through weak ionic interactions. The purified precursor displayed the same catalytic properties as levansucrase secreted by B. subtilis. Thus yeast could be used as a source of levansucrase precursor allowing its isolation as a pure form on a milligram scale.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100104
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    The targeting of bacillus subtilis levansucrase in yeast is correlated to both the hydrophobicity of the signal peptide and the net charge of the N-terminus mature part (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 953-963 
    Details
    ISSN: 0749-503X
    Keywords: Heterologous gene expression ; levansucrase ; signal peptide ; B. subtilis ; S. cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We compared the ability of signal sequences from various Bacillus or yeast secreted proteins to direct Bacillus subtilis levansucrase into the secretion pathway of the yeast Saccharomyces cerevisiae. The efficiency of these sequences correlated with the overall hydrophobicity of their h-domain and was independent of their origin. Furthermore, the net charge of the proximal protein sequence downstream from the signal sequence contributed to the competence of the heterologous proteins to be secreted by yeast. Modification of this net charge allowed the protein to be translocated under the control of the yeast invertase signal sequence. Moreover, glycosylation of levansucrase did not modify significantly the fructosyl polymerase activity.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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