TY - JOUR
A1 - Goebel, Werner
A1 - Kreft, Jürgen
T1 - Accumulation of replicative intermediates and catenated forms of the colicinogenic factor E\(_1\) in E. coli during the replication at elevated temperatures
N2 - No abstract available
KW - Biologie
Y1 - 1972
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60625
ER -
TY - JOUR
A1 - Härtlein, Michael
A1 - Schiessl, Sigrid
A1 - Wagner, Wilma
A1 - Rdest, Ursula
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - Transport of hemolysin by Escherichia coli
N2 - No abstract available
KW - Biologie
KW - Hemolysin
KW - Escberichia coli
KW - Gene cloning
KW - Expression
KW - Transport
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60619
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Burger, Klaus J.
A1 - Goebel, Werner
T1 - Expression of antibiotic resistance genes from Escherichia coli in Bacillus subtilis
N2 - 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.
KW - Biologie
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60600
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Berger, Harald
A1 - Härtlein, Michael
A1 - Müller, Bodo
A1 - Weidinger, Gerhard
A1 - Goebel, Werner
T1 - Cloning and expression in Escherichia coli and Bacillus subtilis of the hemolysin (cereolysin) determinant from Bacillus cereus
N2 - 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 repücates 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 üsteriolysin-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.
KW - Biologie
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60596
ER -
TY - JOUR
A1 - Gilmore, Michael S.
A1 - Cruz-Rodz, Armando L.
A1 - Leimeister-Wächter, Michaela
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage
N2 - 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.
KW - Biologie
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60588
ER -
TY - JOUR
A1 - Schülein, Ralf
A1 - Kreft, Jürgen
A1 - Gonski, Sigrid
A1 - Goebel, Werner
T1 - Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme
N2 - 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.
KW - Biologie
KW - Bacillus
KW - Proenzyme
KW - Subtilisin maturation
KW - Site-directed mutagenesis
KW - Subtilisin Carlsberg
Y1 - 1991
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60577
ER -
TY - JOUR
A1 - Goebel, Werner
A1 - Kathariou, S.
A1 - Kuhn, M.
A1 - Sokolovic, Z.
A1 - Kreft, Jürgen
A1 - Köhler, S.
A1 - Funke, D.
A1 - Chakraborty, T.
A1 - Leimeister-Wächter, M.
T1 - Hemolysin from Listeria-biochemistry, genetics and function in pathogenesis
N2 - No abstract available
KW - Biologie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60563
ER -
TY - JOUR
A1 - Goebel, Werner
A1 - Chakraborty, T.
A1 - Kreft, Jürgen
T1 - Bacterial hemolysins as virulence factors
N2 - No abstract available
KW - Biologie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60553
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Funke, Dorothee
A1 - Haas, Albert
A1 - Lottspeich, Friedrich
A1 - Goebel, Werner
T1 - Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.
N2 - 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.
KW - Biologie
KW - Hemolysin
KW - Listeria
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60545
ER -
TY - JOUR
A1 - Haas, Albert
A1 - Brehm, Klaus
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases
N2 - 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.
KW - Biologie
Y1 - 1991
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60536
ER -