Dokument-ID Dokumenttyp Verfasser/Autoren Herausgeber Haupttitel Abstract Auflage Verlagsort Verlag Erscheinungsjahr Seitenzahl Schriftenreihe Titel Schriftenreihe Bandzahl ISBN Quelle der Hochschulschrift Konferenzname Quelle:Titel Quelle:Jahrgang Quelle:Heftnummer Quelle:Erste Seite Quelle:Letzte Seite URN DOI Abteilungen OPUS4-5045 Wissenschaftlicher Artikel Brehm, Klaus; Haas, Albert; Goebel, Werner; Kreft, Jürgen A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes 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. 1992 urn:nbn:de:bvb:20-opus-60515 Theodor-Boveri-Institut für Biowissenschaften OPUS4-5046 Wissenschaftlicher Artikel Haas, Albert; Dumbsky, Martina; Kreft, Jürgen Listeriolysin genes: complete sequence of ilo from Listeria ivanovii and of lso from Listeria seeligeri The completc DNA scqucnccs coding for thc thiol-activated cytolysins from Listeria ivanovii, ivanolysin 0 (ILO) and for sccligerolysin 0 (LSO) from Listeria seeligeri have been dctermined. Thc deduced amino acid scquences revealed that: (i) the primary translation products comprise 528 (ILO) and 530 (LSO) amino acids. respectively. (ii) ILO contains two cysteines. LSO has a substitution in the conserved cysteine motif. 1992 urn:nbn:de:bvb:20-opus-60529 Theodor-Boveri-Institut für Biowissenschaften OPUS4-5047 Wissenschaftlicher Artikel Haas, Albert; Brehm, Klaus; Kreft, Jürgen; Goebel, Werner Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases 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. 1991 urn:nbn:de:bvb:20-opus-60536 Theodor-Boveri-Institut für Biowissenschaften OPUS4-5067 Wissenschaftlicher Artikel Kreft, Jürgen; Funke, Dorothee; Haas, Albert; Lottspeich, Friedrich; Goebel, Werner Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b. 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. 1989 urn:nbn:de:bvb:20-opus-60545 Theodor-Boveri-Institut für Biowissenschaften