@article{LampidisGrossSokolovicetal.1994,
author = {Lampidis, Robert and Gross, Roy and Sokolovic, Zeljka and Goebel, Werner and Kreft, J{\"u}rgen},
title = {The virulence regulator protein of Listeria ivanovii is highly homologous to PrfA from Listeria monocytogenes and both belong to the Crp-Fnr family of transcription regulators},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60503},
year = {1994},
abstract = {No abstract available},
subject = {Biologie},
language = {en}
}
@article{BrehmHaasGoebeletal.1992,
author = {Brehm, Klaus and Haas, Albert and Goebel, Werner and Kreft, J{\"u}rgen},
title = {A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60515},
year = {1992},
abstract = {A gene (Imsod) encoding superoxide dismutase (SOD; EC 1.15.1.1) of the facultative intracellular pathogen, Listeria monocytogenes, was cloned by functional complementation of an SOD-deficient Escherichia coli mutant. The nucleotide sequence was determined and the deduced amino acid (aa) sequence (202 aa) showed close similarity to manganese-containing SOD's from other organisms. Subunits of the recombinant L. monocytogenes SOD (re-SOD) and of both E. coli SODs formed enzymatically active hybrid enzymes in vivo. DNA/DNA-hybridization experiments showed that this type of recombinant re-sod gene is conserved within the genus Listeria.},
subject = {Biologie},
language = {en}
}
@article{HaasBrehmKreftetal.1991,
author = {Haas, Albert and Brehm, Klaus and Kreft, J{\"u}rgen and Goebel, Werner},
title = {Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60536},
year = {1991},
abstract = {A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the grain-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DHSa as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately SO times that of the combined E. coli catalases. The nucleutide sequence was determined, and the deduced amino acid sequence revealed 43.2\% amino acid sequence identity between bovine liver catalase and L. seeligeri catalase. Most of the amino acid residues which are involved in catalytic activity, the formation of the active center accession channel, and heme binding in bovine liver catalase were also present in L. seeligeri catalase at the corresponding positions. The recombinant protein contained 488 amino acid residues and had a calculated molecular weight of 55,869. The predicted isoelectric point was 5.0. Enzymatic and genetic analyses showed that there is most probably a single catalase of this type in L. seeligeri. A perfect 21-bp inverted repeat, which was highly homologous to previously reported binding sequences of the Fur (ferric uptake regulon) protein of E. coli, was detected next to the putative promoter region of tbe L. seeligeri catalase gene.},
subject = {Biologie},
language = {en}
}
@article{SchueleinKreftGonskietal.1991,
author = {Sch{\"u}lein, Ralf and Kreft, J{\"u}rgen and Gonski, Sigrid and Goebel, Werner},
title = {Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60577},
year = {1991},
abstract = {During an investigation into the substrate specificity and processing of subtilisin Carlsberg from Bacillus licheniformis, two major independent findings were made: (i) as has been shown previously, a stretch of five amino acids (residues 97-101 of the mature enzyme) that loops out into the binding cleft is involved in substrate binding by subtilisin Carlsberg. In order to see whether this loop element also determines substrate specificity, the coding region for these five amino acids was deleted from the cloned gene for subtilisin Carlsberg by site-directed mutagenesis. Unexpectedly the resulting mutant preproenzyme (P42c, Mr=42 kDa) was not processed to the mature form (Mr = 30 kDa) and was not released into the medium by a proteasedeficient B. subtilis host strain; rather, it accumulated in the cell membrane. This result demonstrates that the integrity of this loop element, which is very distant from the processing cleavage sites in the preproenzyme, is required for secretion of subtilisin Carlsberg. (ii) In culture supernatants from B. subtilis harbouring the cloned wild-type subtilisin Carlsberg gene the transient appearance (at 0-3 h after onset of stationary phase) of a processing intermediate (P38c, Mr = 38 kDa) oftbis protease could be demonstrated. P38c very probably represents a genuine proform of subtilisin Carlsberg.},
subject = {Biologie},
language = {en}
}
@article{KreftFunkeHaasetal.1989,
author = {Kreft, J{\"u}rgen and Funke, Dorothee and Haas, Albert and Lottspeich, Friedrich and Goebel, Werner},
title = {Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60545},
year = {1989},
abstract = {In culture supematants of both Listeria ivanovii and Listeria monocytogenes Sv4b, for the first time a hemolysin of molecular weight 58 kDa was identified, which had all the characteristics of an SH-activated cytolysin, and which was therefore identified as Iisteriolysin 0 (LLO). In the case of L. ivanovii a second major supematant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supematants of L. ivanovii a sphingomyelinase and a Iecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-tenninal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.},
subject = {Biologie},
language = {en}
}
@article{GilmoreCruzRodzLeimeisterWaechteretal.1989,
author = {Gilmore, Michael S. and Cruz-Rodz, Armando L. and Leimeister-W{\"a}chter, Michaela and Kreft, J{\"u}rgen and Goebel, Werner},
title = {A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60588},
year = {1989},
abstract = {A cloned cytolytic determinant from the genome of Bacillus cereus GP-4 has been characterized at the molecular Ievel. Nucleotide sequence determination revealed the presence of two open reading frames. 8oth open reading frames were found by deletion and complementation analysis to be necessary for expression of the hemolytic phenotype by Bacillus subtilis and Escherichia coli hosts. The 5' open reading frame was found to be nearly identical to a recently reported phospholipase C gene derived from a mutant B. cereus strain which overexpresses the respective protein, and it conferred a lecithinase-positive phenotype to the B. subtilis host. The 3' open reading frame encoded a sphingomyelinase. The two tandemly encoded activities, phospholipase C and sphingomyelinase, constitute a biologically functional cytolytic determinant of B. cereus termed cereolysin AB.},
subject = {Biologie},
language = {en}
}
@article{GoebelChakrabortyKreft1988,
author = {Goebel, Werner and Chakraborty, T. and Kreft, J{\"u}rgen},
title = {Bacterial hemolysins as virulence factors},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60553},
year = {1988},
abstract = {No abstract available},
subject = {Biologie},
language = {en}
}
@article{GoebelKathariouKuhnetal.1988,
author = {Goebel, Werner and Kathariou, S. and Kuhn, M. and Sokolovic, Z. and Kreft, J{\"u}rgen and K{\"o}hler, S. and Funke, D. and Chakraborty, T. and Leimeister-W{\"a}chter, M.},
title = {Hemolysin from Listeria-biochemistry, genetics and function in pathogenesis},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60563},
year = {1988},
abstract = {No abstract available},
subject = {Biologie},
language = {en}
}
@article{KreftBurgerGoebel1983,
author = {Kreft, J{\"u}rgen and Burger, Klaus J. and Goebel, Werner},
title = {Expression of antibiotic resistance genes from Escherichia coli in Bacillus subtilis},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60600},
year = {1983},
abstract = {Bifunctional recombinant plasmids were constructed, comprised of the E. coli vectors pBR322, pBR325 and pACYC184 and different plasmids from Gram-positive bacteria, e.g. pBSU161-1 of B. subtilis and pUB110 and pC221 of S. aureus. The beta-lactamase (bla) gene and the chloramphenicol acetyltransferase (cat) gene from the E. coli plasmids were not transcribed and therefore not expressed in B. subtilis. However, tetracycline resistance from the E. coli plasmids was expressed in B. subtilis. Transcription of the tetracycline resistance gene(s) started in B. subtilis at or near the original E. coli promoter, the sequence of which is almost identical with the sequence recognized by σ55 of B. subtilis RNA polymerase.},
subject = {Biologie},
language = {en}
}
@article{KreftBergerHaertleinetal.1983,
author = {Kreft, J{\"u}rgen and Berger, Harald and H{\"a}rtlein, Michael and M{\"u}ller, Bodo and Weidinger, Gerhard and Goebel, Werner},
title = {Cloning and expression in Escherichia coli and Bacillus subtilis of the hemolysin (cereolysin) determinant from Bacillus cereus},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60596},
year = {1983},
abstract = {From a cosmid gene bank of Bacillus cereus GP4 in Escherichia coli we isolated clones which, after several days of incubation, formed hemolysis zones on erythrocyte agar plates. These clones contained recombinant cosmids with B. cereus DNA insertions of varying lengths which shared some common restriction fragments. The smallest insertionwas recloned as aPstl fragment into pJKK3-1, a shuttle vector which rep{\"u}cates in Bacillus subtilis and E. coli. When this recombinant plasmid (pJKK3-1 hly-1) was transformed into E. coli, it caused hemolysis on erythrocyte agar plates, but in liquid assays no extemal or intemal hemolytic activity could be detected with the E. coli transformants. B. subtilis carrying the same plasmid exhibited hemolytic activity at Ievels comparable to those ofthe B. cereus donor strain. The hemolysin produced in B. subtilis seemed to be indistinguishable from cereolysin in its sensitivity to cholesterol, activation by dithiothreitol, and inactivation by antibodies raised against cereolysin. When the recombinant DNA carrying the cereolysin gene was used as a probe in hybridization experiments with chromosomal DNA from a streptolysin 0-producing strain of Streptococcus pyogenes or from {\"u}steriolysin-producing strains of Usteria monoeytogenes, no positive hybridization signals were obtained. These data soggest that the genes for these three SH-activated cytolysins do not have extended sequence homology.},
subject = {Biologie},
language = {en}
}
@article{HaertleinSchiesslWagneretal.1983,
author = {H{\"a}rtlein, Michael and Schiessl, Sigrid and Wagner, Wilma and Rdest, Ursula and Kreft, J{\"u}rgen and Goebel, Werner},
title = {Transport of hemolysin by Escherichia coli},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60619},
year = {1983},
abstract = {No abstract available},
subject = {Biologie},
language = {en}
}
@article{GoebelKreft1972,
author = {Goebel, Werner and Kreft, J{\"u}rgen},
title = {Accumulation of replicative intermediates and catenated forms of the colicinogenic factor E\(_1\) in E. coli during the replication at elevated temperatures},
url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60625},
year = {1972},
abstract = {No abstract available},
subject = {Biologie},
language = {en}
}