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  • 1985-1989  (6)
  • 1975-1979  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Identification of a new locus, sacV, involved in the regulation of levansucrase synthesis in Bacillus subtilis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 44 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An EcoRI DNA fragment of 0.5 kb specifically stimulating levansucrase synthesis was cloned in Bacillus subtilis. Transcriptional stimulation of levansucrase expression was observed after induction by sucrose when the sequence was present on a multicopy plasmid in B. subtilis. The nucleotide sequence of the DNA fragment was determined. The involvement of a putative peptide is discussed. This fragment located on the chromosomal map of B. subtilis near the dal locus defines a new locus, sacV, of the sucrose metabolic system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02238.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning of the sacS gene encoding a positive regulator of the sucrose regulon in Bacillus subtilis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 41 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The sacS gene controls the expression of 2 saccharolytic enzymes in Bacillus subtilis (sucrase and levansucrase).This paper describes a recombinant plasmid containing a mutant allele, sacSc. The plasmid was isolated from a B. subtilis DNA bank established in Escherichia coli. Moreover, it was shown that the sacSc allele, placed on a high-copy plasmid, is dominant over the wild-type chromosomal sacS+ allele. This result strongly suggests that the sacS gene encodes a positive regulatory protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02184.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A system for the inducible secretion of proteins from Bacillus subtilis during logarithmic growth (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 52 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A Bacillus subtilis-Escherichia coli shuttle vector was constructed containing the B. subtilis levansucrase gene promoter and region encoding its signal sequence.A site for the restriction enzyme NaeI was included to facilitate precise translational fusions to the DNA encoding the levansucrase signal sequence. Fusions of TEM β-lactamase to this construct displayed sucrose-inducible expression and secretion of B. subtilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02581.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase (1987)
    Springer
    Molecular genetics and genomics 208 (1987), S. 177-184 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus subtilis ; Levanase ; Nucleotide sequence ; Yeast invertase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The structural gene for the enzyme levanase of Bacillus subtilis (SacC) was cloned in Escherichia coli. The cloned gene was mapped by PBS1 transduction near the sacL locus on the B. subtilis chromosome, between leu4 and aroD. Expression of the enzyme was demonstrated both in B. subtilis and in E. coli. The presence of sacC allowed E. coli to grow on sucrose as the sole carbon source. The complete nucleotide sequence of sacC was determined. It includes an open reading frame of 2,031 bp, coding for a protein with calculated molecular weight of 75,866 Da, including a putative signal peptide similar to precursors of secreted proteins found in Bacilli. The apparent molecular weight of purified levanase is 73 kDa. The sacC gene product was characterized in an in vitro system and in a minicellproducing strain of E. coli, confirming the existence of a precursor form of levanase of about 75 kDa. Comparison of the predicted aminoacid sequence of levanase with those of the two other known β-D-fructofuranosidases of B. subtilis indicated a homology with sucrase, but not with levansucrase. A stronger homology was detected with the N-terminal region of yeast invertase, suggesting the existence of a common ancestor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330439
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Specificity of action on mosquito larvae of Bacillus thuringiensis israelensis toxins encoded by two different genes (1988)
    Springer
    Molecular genetics and genomics 214 (1988), S. 42-47 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus thuringiensis israelensis ; Gene for 130 kDa protein ; Synergism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 135 kDa protein gene and two open reading frames (ORF1 and ORF2) have been cloned from a large plasmid of Bacillus thuringiensis israelensis (Bourgouin et al. 1986). The Escherichia coli recombinant clones containing these genes were highly toxic to larvae of Aedes aegypti, Anopheles stephensi and Culex pipiens. From subcloning experiments it was deduced that the 135 kDa polypeptide alone was responsible for the toxic activity on both A. aegypti and An. stephensi larvae. In contrast, the presence of two polypeptides, the 135 kDa protein and the ORF1 product was required for toxicity to C. pipiens larvae. The minimal toxic fragment of the 135 kDa polypeptide has been delineated. The results indicate that a polypeptide of about 65 kDa, corresponding to an amino-terminal part of the 135 kDa protein is sufficient for toxicity. Sequence comparisons indicate that the ORF1 product may correspond to an N-terminal part of a rearranged 130 kDa protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00340177
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Construction of a colony bank of E. coli containing hybrid plasmids representative of the Bacillus subtilis 168 genome (1979)
    Springer
    Molecular genetics and genomics 176 (1979), S. 239-245 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A collection of about 2500 clones containing hybrid plasmids representative of nearly the entire genome of B. subtilis 168 was established in E. coli SK1592 by using the poly(dA)·poly(dT) joining method with randomly sheared DNA fragments and plasmid pHV33, a bifunctional vector which can replicate in both E. coli and B. subtilis. Detection of cloned recombinant DNA molecules was based on the insertional inactivation of the Tc gene occurring at the unique BamHI cleavage site present in the vector plasmid. Thirty individual clones of the collection were shown to hybridize specifically with a B. subtilis rRNA probe. CCC-recombinant plasmids extracted from E. coli were pooled in lots of 100 and used to transform auxotrophic mutants of B. subtilis 168. Complementation of these auxotrophic mutations was observed for several markers such as thr, leuA, hisA, glyB and purB. In several cases, markers carried by the recombinant plasmids were lost from the plasmid and integrated into the chromosomal DNA. Loss of genetic markers from the hybrid plasmids did not occur when a rec - recipient strain of B. subtilis was used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273218
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of the genes encoding the haemolytic toxin and the mosquitocidal delta-endotoxin of Bacillus thuringiensis israelensis (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 390-397 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus thuringiensis israelensis ; Toxin genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The crystalline parasporal inclusions (crystals) of Bacillus thuringiensis israelensis (Bti), which are specifically toxic to mosquito and black fly larvae, contain three main polypeptides of 28 kDa, 68 kDa and 130 kDa. The genes encoding the 28 kDa protein and the 130 kDa protein have been cloned from a large plasmid of Bti. Escherichiacoli recombinant clones containing the 130 kDa protein gene were highly active against larvae of Aedes aegypti and Culex pipiens, while B. subtilis recombinant cells containing the 28 kDa protein gene were haemolytic for sheep red blood cells. A fragment of the Bti plasmid which is partially homologous to the 130 kDa protein gene was also isolated; it probably corresponds to part of a second type of mosquitocidal toxin gene. Furthermore, restriction enzyme analysis suggested that the 130 kDa protein gene is located on the same Bti EcoRI fragment as another kind of Bti mosquitocidal protein gene cloned by Thorne et al. (1986). Hybridization experiments conducted with the 28 kDa protein gene and the 230 kDa protein gene showed that these two Bti genes are probably present in the plasmid DNA of B. thuringiensis subsp. morrisoni (PG14), which is also highly active against mosquito larvae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00338072
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    Paper (German National Licenses)
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