- Volume 142, Issue 11, 1996
Volume 142, Issue 11, 1996
- Review Article
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- Microbiology Comment
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- Antigens And Immunity
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Sequence variability of FrpB, a major iron-regulated outer-membrane protein in the pathogenic neisseriae
More LessThe FrpB protein from pathogenic neisseriae is a 77 kDa iron-regulated outer-membrane protein that belongs to the family of TonB-dependent receptors and may have potential as a vaccine component. Comparison between the frpB gene from three different meningococcal strains and a published gonococcal one revealed that the region from residues 350 to 390 displays pronounced sequence variability. In a model for the topology of FrpB in the outer membrane, this region corresponds to loop 7, the longest of the predicted 13 surface-exposed loops. Binding of four out of a total of eight bactericidal monoclonal antibodies to synthetic peptides corresponding to loop 7 showed that their epitopes are located here. The frpB genes from five additional meningococcal strains were cloned and sequenced in this region. Pairwise comparisons showed different degrees of similarity.
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- Biochemistry
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Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
More LessWe have characterized the substrate specificity of dimethyl sulfoxide reductase (DmsABC) of Escherichia coli by determining K m and k cat values for 22 different substrates. The enzyme has a very broad substrate specificity. The K m values varied 470-fold, while k cat values varied only 20-fold, implicating K m as the major determinant of k cat/K m values. Sulfoxides and pyridine N-oxide exhibited the lowest K m values, followed by aliphatic N-oxides. The k cat values for these compounds also followed the same pattern. Substitution at the 2 or 3 position of the pyridine N-oxide ring had little effect on K m’ while substitution at the 4 position had a greater effect, and increased K m. Negatively charged substrates were poorly accepted. A few compounds that are not S- or N-oxides were also reduced by the enzyme. Most compounds reduced by DmsABC were not toxic to E. coli under anaerobic growth conditions, and E. coli was able to use many of these compounds anaerobically as terminal electron acceptors in the presence of glycerol. Anaerobic growth on sulfoxides is solely due to DmsABC expression. However, there appears to be another as yet unidentified terminal reductase capable of using pyridine N-oxides as terminal electron acceptors.
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- Environmental Microbiology
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Studies on the isopropylbenzene 2,3-dioxygenase and the 3-isopropylcatechol 2,3-dioxygenase genes encoded by the linear plasmid of Rhodococcus erythropolis BD2
More LessThe enzymes responsible for the degradation of isopropylbenzene (IPB) and co-oxidation of trichloroethene (TCE) by Rhodococcus erythropolis BD2 are encoded by the linear plasmid pBD2. Fragments containing IPB catabolic genes were cloned from pBD2 and the nucleotide sequence was determined. By means of database searches and expression of the cloned genes in recombinant strains, we identified five clustered genes, ipbA1A2A3A4C, which encode the three components of the IPB 2,3-dioxygenase system, reductaseIPB (ipbA4), ferredoxinIPB (ipbA3) and the two subunits of the terminal dioxygenase (ipbA1A2), as well as the 3-isopropylcatechol (IPC) 2,3-dioxygenase (ipbC). The protein sequences deduced from the ipbA1A2A3A4C gene cluster exhibited significant homology with the corresponding proteins of analogous degradative pathways in Gram-negative and Gram-positive bacteria, but the gene order differed from most of them. IPB 2,3-dioxygenase and 3-IPC 2,3-dioxygenase could both be expressed in Escherichia coli, but the IPB 2,3-dioxygenase activities were too low to be detected by polarographic and TCE degradative means. However, inhibitor studies with the R. erythropolis BD2 wild-type are in accordance with the involvement of the IPB 2,3-dioxygenase in TCE oxidation.
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- Genetics And Molecular Biology
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Immunochemical structure of the OmpD porin from Salmonella typhimurium
More LessThe OmpD porin was isolated and purified from Salmonella typhimurium strain SH 7454 (ompC::Tn10), digested with cyanogen bromide (CNBr) and the peptide fragments were separated by SDS-PAGE. N-terminal sequencing identified a total of 96 residues from four distinct peptides. The sequence showed that OmpD is homologous to NmpC (75% identity), Lc (75%) and OmpC (70%) from Escherichia coli, and OmpC (68%) from S. typhimurium. The sequence was essentially identical to the translated sequence of an nmpC-like gene of S. typhimurium, currently placed at 38·6 centisomes of the chromosome. Our results and other data suggest, however, that this gene is actually the ompD gene, which is more correctly placed in the 34 centisome region of the chromosome. The CNBr-generated peptides were also screened with 16 anti-S. typhimurium OmpD monoclonal antibodies by Western blotting. These results, in conjunction with the prediction of the OmpD folding pattern based on the known three-dimensional structure of E. coli OmpF, showed a close immunological relationship among S. typhimurium OmpD and E. coli NmpC and Lc, and a strong conservation of sequences within the transmembrane β strands of these porins and E. coli OmpC, PhoE and OmpF, and Salmonella typhi OmpC.
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hymA (hypha-like metulae), a new developmental mutant of Aspergillus nidulans
More LessAsexual fruiting body development in Aspergillus nidulans requires a precise spatial and temporal coordinated expression of many genes. Insertional mutagenesis was used to isolate and characterize a new mutant of A. nidulans in which hyphal growth was slightly reduced and conidiophore development was specifically blocked at the metula stage. In contrast to the uninucleate metulae of the wild-type, in the mutant these structures were elongated, multinucleate and septate. Further differentiation and production of phialides by a budding-like process was not observed. The mutant metulae thus resembled hyphae rather than metulae and the gene was therefore named hypha-like metulae (hymA). The hymA gene was mapped to linkage group VI. The integrated vector was rescued with border sequences from the integration site. The border sequences were used to isolate a cosmid from a wild-type library which was subcloned to a 5 kb fragment able to complement the mutation in trans. This fragment encoded a 1·8 kb transcript expressed in hyphae and throughout development. It is proposed that hymA is involved in budding processes, and is required for the formation of metulae and for their further differentiation.
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The purB gene of Escherichia coli K-12 is located in an operon
More LessThe structural gene (purB) for succinyl-AMP (S-AMP) lyase and three additional ORFs are on the same DNA strand of the chromosome of Escherichia coli. Cassette mutagenesis and primer extension mapping demonstrated that purB is co-transcribed with an upstream gene (ORF23, or ycfC) encoding a 22·9 kDa membrane-associated protein of non-essential, but unknown, function unrelated to purine biosynthesis. The purB operon lies between phoP and an ORF expressing an essential function which may correspond to asuE (trmU). S-AMP lyase was purified to near homogeneity. The purified enzyme is a homotetramer of 50 kDa subunits, has a K m for S-AMP of 3·7 μM and a pH optimum of 7·4–7·6.
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Proline biosynthesis in Streptococcus thermophilus: characterization of the proBA operon and its products
More LessThe presence of proline in the medium was not essential for growth of Streptococcus thermophilus, indicating that there is a proline biosynthetic pathway in this organism. Genetic and biochemical analysis identified and characterized this pathway. Two genes, designated proB and proA, were cloned, sequenced and characterized. Biochemical analysis of the proB- and proA-encoded enzymes showed that the proline biosynthetic pathway of S. thermophilus is similar to the one previously described in Escherichia coli. The deduced amino acid sequence of a 2·408 kb DNA region containing the genes revealed the similarity of the S. thermophilus gene products to ProB and ProA of E. coli and Serratia marcescens, and to the corresponding N- and C-terminal domains of the bifunctional plant enzyme Δ1-pyrroline-5-carboxylate synthetase of Vigna aconitifolia. Northern blot analysis showed that the two genes in S. thermophilus are organized in a single operon with proB proximal and proA distal to the promoter; primer extension analysis indicated that proBA transcription is not under repressive control by exogenously supplied proline.
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RP4::Mu3A-mediated in vivo cloning and transfer of a chlorobiphenyl catabolic pathway
Chromosomal DNA fragments encoding the ability to utilize biphenyl as sole carbon source (Bph+) were mobilized by means of plasmid RP4::Mu3A from strain JB1 (tentatively identified as Burkholderia sp.) to Alcaligenes eutrophus CH34 at a frequency of 10−8 per transferred plasmid. The mobilized DNA integrated into the recipient chromosome or was recovered as catabolic prime plasmids. Three Bph+ prime plasmids were transferred from A. eutrophus to Escherichia coli and back to A. eutrophus without modification of the phenotype. The transferred Bph+ DNA segments allowed metabolism of biphenyl, 2-, 3- and 4-chlorobiphenyl, and diphenylmethane. Genes involved in biphenyl degradation were identified on the prime plasmids by DNA-DNA hybridization and by gene cloning. Bph+ prime plasmids were transferred to Burkholderia cepacia, Pseudomonas aeruginosa, Comamonas testosteroni and A. eutrophus and the catabolic genes were expressed in those hosts. Transfer of the plasmid to the 3-chlorobenzoate-degrading bacterium Pseudomonas sp. B13 allowed the recipient to mineralize 3-chlorobiphenyl. Other catabolic prime plasmids were obtained from JB1 by selection on m-hydroxybenzoate and tyrosine as carbon sources. 16S rRNA sequence data demonstrated that the in vivo transfer of bph was achieved between bacteria belonging to two different branches of the β-Proteobacteria.
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Complete sequence and organization of the Serratia marcescens biotin operon
More LessThe nucleotide sequence of the biotin (bio) operon of wild-type Serratia marcescens Sr41 was determined. Five ORFs were identified to encode BioA (7,8-diaminopelargonic acid aminotransferase), BioB (biotin synthase), BioF (7-keto-8-aminopelargonic acid synthase), BioC (an enzyme catalysing the synthesis of pimeloyl-CoA) and BioD (dethiobiotin synthase), in this order. The operon was deduced to be transcribed divergently to the left into bioA and to the right into the bioBFCD genes. The promoters and a common predicted operator for both bioA and bioBFCD genes were located between the bioA and bioB genes. The predicted amino acid sequences of these enzymes were similar to the sequences of the corresponding enzymes of Escherichia coli. Analysis of expression of the lacZ structural gene fused with the bioA and bioB promoters revealed that the biotin operon was subject to biotin-mediated feedback repression.
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KatP, a novel catalase-peroxidase encoded by the large plasmid of enterohaemorrhagic Escherichia coli O157:H7
More LessA gene coding for a catalase-peroxidase activity was identified on a 9·7 kb Smal DNA fragment derived from the large plasmid p0157 of enterohaemorrhagic Escherichia coli (EHEC) 0157:H7 strain EDL 933. Nucleotide sequencing revealed an ORF of 2208 bp and predicted a 736 amino acid polypeptide with a molecular mass of 81·8 kDa. This putative protein was found to be highly homologous to members of the bacterial bifunctional catalase-peroxidase family. Analysis of its amino acid sequence revealed the presence of characteristic peroxidase 1 and 2 motifs. In addition, an N-terminal signal sequence was found, suggesting that the catalase-peroxidase is transported through the cytoplasmic membrane. EHEC catalase-peroxidase activities were investigated in cytoplasmic and periplasmic crude extracts as well as in culture supernatants from wild-type and recombinant E. coli strains. EHEC-specific catalase-peroxidase activity was detected primarily in the periplasm in strain EDL 933. The newly discovered enzyme was designated KatP, to indicate its plasmid origin. PCR analysis of representative strains of all enteric E. coli pathogroups (i.e. enterohaemorrhagic, enterotoxigenic, enteropathogenic, enteroaggregative and enteroinvasive E. coli) revealed a close association between the occurrence of EHEC-haemolysin and the katP gene in Shiga-like-toxin-producing E. coli 0157 strains.
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- Pathogenicity And Medical Microbiology
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Role of the Bordetella pertussis P.69/pertactin protein and the P.69/pertactin RGD motif in the adherence to and invasion of mammalian cells
The role of the Bordetella pertussis P.69/pertactin protein in mammalian cell adhesion and invasion was investigated. Salmonella strains expressing surface-associated P.69/pertactin from a chromosomally located prn gene were significantly more invasive than isogenic parental strains. This effect was most pronounced in the poorly invasive, semi-rough S. typhimurium strain LB5010. Escherichia coli K-12 strain HB101 harbouring the plasmid p41869D, which encodes the full-length prn gene under the control of the tac promoter on the broad-host-range plasmid pMMB66EH, was significantly more adhesive to HEp-2 and Chinese Hamster Ovary (CHO) cells growing in culture than E. coli HB101(pMMB66EH). However, the ability of E. coli to invade mammalian cells was not affected by P.69/pertactin expression. P.69/pertactin-mediated adhesiveness of HB101 to HEp-2 and CHO cells was not influenced by the viability of the bacterial cells. However, adherence was markedly reduced when assays were performed for less than 3 h, at 4°C or in the presence of cycloheximide, suggesting the active participation of the eukaryotic cell in bacterial adhesion. Site-directed mutagenesis was used to mutate Asp to Glu in an Arg-Gly-Asp (RGD→RGE) sequence present in mature P.69/pertactin and the mutated gene was cloned in the same broad-host-range vector (plasmid p41869E). This mutation had no detectable influence on the ability of P.69/pertactin to mediate adhesion of HB101 to HEp-2 or CHO cells. Plasmids p41869D and p41869E were introduced into the bvg-negative B. pertussis strain BP347. Expression of P.69RGD or P.69RGE did not enhance the adhesiveness of BP347 for epithelial (HEp-2 and CHO) cells.
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- Physiology And Growth
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Phosphate-starvation-inducible proteins in Bacillus subtilis: a two-dimensional gel electrophoresis study
More LessA two-dimensional (2-D) gel electrophoresis study of Bacillus subtilis strain 168 identified 20 proteins that are strongly induced in response to phosphate starvation. The induction of nine of these phosphate-starvation-induced (Psi) proteins was dependent on a functional PhoR protein. PhoR is the histidine sensor-kinase component of a phosphate-concentration-sensing two-component regulatory system which, together with its partner response regulator PhoP, controls the expression of genes in the Pho regulon. Genes encoding PhoR-dependent Psi proteins are therefore likely to be members of the Pho regulon. SpoOA ~ P, the response regulator of the signal transduction pathway required for the induction of sporulation, has previously been shown to negatively affect the induction of the Pho regulon by repressing the phoP-phoR operon. The induction pattern of some PhoR-dependent Psi proteins was altered in a spoOA mutant such that their synthesis continued for longer than was found with the wild-type. The most abundant Psi protein, Psi1–3, was characterized by N-terminal sequencing of internal peptide fragments and shown to have a high similarity to an Escherichia coli protein which is involved in phosphate uptake during phosphate starvation.
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Changes in cell morphology and carnitine acetyltransferase activity in Candida albicans following growth on lipids and serum and after in vivo incubation in mice
More LessCandida albicans C316, maintained in the yeast form, showed a proliferation of peroxisomes when grown on triolein or serum as sole carbon source but these structures were absent from glucose-grown cells. Peroxisomes were also apparent in C. albicans obtained after injection into mice and recovery from intraperitoneal washings and kidneys; they may therefore be useful markers to assess a potential in vivo response in cells that are growing in vitro. Trans-cell-wall structures also occurred in C. albicans grown on triolein or serum, and in cells cultured in vivo, but were not seen in cells grown on glucose. These structures consisted of electron-dense fibrillar material penetrating through the cell wall from the plasmalemma side and protruded out to the exterior of the cell. Endoplasmic reticulum, located at the periphery of the cell, was found to be in close proximity with these cell wall structures. Carnitine acetyltransferase (CAT; EC 2.3.1.7), the key enzyme for the translocation of acetyl units between intracellular compartments, was present in low activities in glucose-grown cells; its activity was increased some 100-fold in triolein-grown cells but only 4-fold in serum-grown cells. It was not possible to assess this activity in the in vivo-cultured cells. Two separate CAT proteins, partially purifed from isolated microchondria and peroxisomes, respectively, were identified, with different specificities and kinetic properties.
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Organic acid excretion by Streptomyces lividans TK24 during growth on defined carbon and nitrogen sources
More LessCultures of Streptomyces lividans TK24 grown in defined media containing certain rapidly used carbon and nitrogen sources excreted high levels of organic acids. These were identified by HPLC and enzymic assays as pyruvic acid and 2-oxoglutaric acid. Acidification occurred only with glucose as the principal carbon source, and depended on the nitrogen source used. With nitrate as the sole nitrogen source, high levels of pyruvate and small amounts of 2-oxoglutarate were produced. Carbon from D-[U-14C]glucose was converted into both organic acids. Combining glucose with a selection of amino acids as primary nitrogen/secondary carbon sources yielded less pyruvate and more 2-oxoglutarate. Carbon from both 14C-labelled glucose and amino acids was metabolized to both organic acids. Adding nitrate to this combination caused a reversion of the acid production pattern to that of the glucose-nitrate combination, as if the amino acids were absent. Addition of ammonium salts to any combination of carbon and nitrogen sources completely prevented organic acid formation.
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Ferric-reductase activities in whole cells and cell fractions of Vibrio (Listonella) anguillarum
More LessThe ability of Vibrio (Listonella) anguillarum strains from serotype groups O1 and O2 to reduce Fe3+ in the form of different chelates was investigated. All strains, grown in M9 minimal medium supplemented with 0·2% Casamino acids, reduced Fe3+ complexed by citrate, nitrilotriacetic acid and EDTA. In whole cells, the degree of reduction was dependent on the Fe3+ ligand and on the strain, with the greatest values corresponding to ferric dicitrate and serotype group O1 strains, respectively. The ferric-reductase activity increased, over the basal levels, when the cells were grown with iron added as ferric dicitrate, haemin or haemoglobin. All strains also reduced ferricyanide, a compound that is not transported into the bacterial cells. Ferricyanide reduction was also increased when the cells were grown in the presence of an iron source. All of the cell fractions (periplasm, membranes and cytoplasm) showed Fe3+-reducing activity, with the highest values observed in the presence of Mg2+, NADH and FAD in the assay buffer. Cytoplasmic ferric-reductase could be visualized using native polyacrylamide or starch gel electrophoresis, whereas the periplasmic and membrane reductase(s) could only be detected on starch gels. The results indicate the presence of different ferric-reductase activities in V. anguillarum, which could be involved in the different iron-acquisition systems present in this micro-organism, i.e. siderophore-mediated systems and siderophore-independent mechanisms.
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The acid tolerance response of Salmonella typhimurium provides protection against organic acids
More LessSalmonella typhimurium encounters a variety of acid stress situations during pathogenesis and in the natural environment. These include the extreme low pH encountered in the stomach and a less acidic intestinal environment containing large amounts of organic weak acids (volatile fatty acids). The acid tolerance response (ATR) is a complex defence system that can minimize the lethal effects of extreme low pH (pH 3). The data presented illustrate that the ATR can also defend against weak acids such as butyric, acetic or propionic acids. Although an acid shock of pH 4·4 induced the ATR, growth in subinhibitory concentrations of weak acids did not. Various mutations shown to affect tolerance to extreme acid conditions (pH 3) were tested for their effects on tolerance to weak acids. An rpoS mutant lacking the alternative sigma factor sS failed to protect cells against weak acids as well as extreme acid pH. The fur (ferric uptake regulator) and atp (Mg2+-dependent ATPase) mutants defective in extreme acid tolerance showed no defects in their tolerance to weak acids. Curiously, the atbR mutant that exhibits increased tolerance to extreme acid pH proved sensitive to weak acids. Several insertions that rendered cells sensitive to organic acids were isolated, all of which proved to be linked to the rpoS locus.
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