127 results found
Charles IG, Dougan G, Pickard D, et al., 1988, Molecular cloning and analysis of P. 69, a vir-controlled protein from Bordetella pertussis., Tokai J Exp Clin Med, Vol: 13 Suppl, Pages: 227-234, ISSN: 0385-0005
The cloning sequencing and analysis of an important antigenic component of Bordetella pertussis is described. The gene for P.69, in common with a variety of other so called "virulence" genes, (e.g., adenylate cyclase (AC), pertussis toxin (PT) and filamentous haemagglutinin (FHA)), is under control of the vir locus. The protein P.69 is externally localised on cells and protein preparations are protective as judged by the mouse intra-cerebral challenge test. The gene encoding the P.69 antigen was isolated by hybridization of mixed oligonucleotide probes against B. pertussis genomic DNA. These oligonucleotides were designed from the protein sequence data obtained from a cyanogen bromide digest of the P.69 protein. DNA sequence analysis reveals a G:C rich gene capable of encoding a protein of 910 amino acids and Mr of 93478, whose likely promoter and ribosome binding sites show little homology to their E.coli counterpart. In common with some of the genes in the PT operon the sequence 5'-CCTGG-3' was found 5' to the ATG initiation codon. At the 3', end 29 bases after the TAA stop codon, the sequence 5'GTTTTTCCT-3' was found in an equivalent position to the same sequence in the PT operon. Examination of the protein sequence reveals two regions with directly repeated elements (GGAVP)3(GGFGP)2 and (PQP)5.
FAIRWEATHER NF, LYNESS VA, MASKELL DJ, 1987, IMMUNIZATION OF MICE AGAINST TETANUS WITH FRAGMENTS OF TETANUS TOXIN SYNTHESIZED IN ESCHERICHIA-COLI, INFECTION AND IMMUNITY, Vol: 55, Pages: 2541-2545, ISSN: 0019-9567
FAIRWEATHER NF, LYNESS VA, 1986, THE COMPLETE NUCLEOTIDE-SEQUENCE OF TETANUS TOXIN, NUCLEIC ACIDS RESEARCH, Vol: 14, Pages: 7809-7812, ISSN: 0305-1048
FAIRWEATHER NF, LYNESS VA, PICKARD DJ, et al., 1986, CLONING, NUCLEOTIDE SEQUENCING, AND EXPRESSION OF TETANUS TOXIN FRAGMENT-C IN ESCHERICHIA-COLI, JOURNAL OF BACTERIOLOGY, Vol: 165, Pages: 21-27, ISSN: 0021-9193
DOUGAN G, FAIRWEATHER N, 1985, GENETIC-ANALYSIS OF GRAM-POSITIVE TOXIN DETERMINANTS - THE IMPACT OF NEW TECHNOLOGIES, MICROBIOLOGICAL SCIENCES, Vol: 2, Pages: 144-147, ISSN: 0265-1351
HERRERO E, FAIRWEATHER NF, HOLLAND IB, 1982, ENVELOPE PROTEIN-SYNTHESIS AND INHIBITION OF CELL-DIVISION IN ESCHERICHIA-COLI DURING INACTIVATION OF THE B-SUBUNIT OF DNA GYRASE, JOURNAL OF GENERAL MICROBIOLOGY, Vol: 128, Pages: 361-369, ISSN: 0022-1287
Fairweather NF, Orr E, Holland IB, 1980, Inhibition of deoxyribonucleic acid gyrase: effects on nucleic acid synthesis and cell division in Escherichia coli K-12., J Bacteriol, Vol: 142, Pages: 153-161, ISSN: 0021-9193
Mutants of Escherichia coli resistant to the antibiotic clorobiocin are also coumermycin resistant, and the mutation to resistance in at least one mutant was mapped near gyrB. We conclude, therefore, that clorobiocin inhibits deoxyribonucleic acid gyrase, and the drug was used to probe the role of this enzyme in vivo. Deozyribonucleic acid synthesis was preferentially inhibited but not completely blocked by the antibiotic. Transcription and cell division were also markedly affected. However, unlike other inhibitors of deoxyribonucleic acid synthesis, clorobiocin failed to induce the synthesis of protein X, the recA gene product. In mutants resistant to clorobiocin the replication velocity was unaffected, but initiation of deoxyribonucleic acid synthesis appeared to be delayed. We conclude that deoxyribonucleic acid gyrase, and hence the supercoiled structure of the chromosome, is important for transcription, normal initiation of deoxyribonucleic acid replication, and cell division. The possible role of deoxyribonucleic acid gyrase in the elongation of replication forks is also discussed.
This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.