Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0519030 (Klebsiella)
 21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During aerobic growth of Escherichia coli ML308 on acetate as sole carbon source, the apparent synthesis of isocitrate dehydrogenase was repressed relative to cultures on other carbon sources, such as glucose, which do not employ the glyoxylate bypass as an anaplerotic sequence. When cells were removed from an acetate medium, or when compounds were added which made the operation of the glyoxylate bypass unnecessary, the activity of isocitrate dehydrogenase rapidly increased 3- to 4-fold but fell again on restoration to an acetate medium. Changes in activity were rapid and, furthermore, could be demonstrated in the absence of protein synthesis. It is thus improbable that the mechanism involved degradation or de novo synthesis of the enzyme protein. Oxaloacetate and glyoxylate showed concerted inhibition of isocitrate dehydrogenase which could be relieved by dialysis. Because extracts of low enzyme activity, derived from acetate-metabolizing cells, could not be stimulated by dialysis or by addition of a wide range of metabolites, it is unlikely that low molecular weight, freely dissociable effectors were responsible for stimulation or inhibition of activity. Control of isocitrate dehydrogenase permitted the efficient utilization of acetate as sole source of carbon and energy but perserved the capacity of the cell to respond rapidly to an improvement in nutritional conditions. A limited survey showed that the mechanism is common but not universal among strains of E. coli and occurs in at least one strain each of Klebsiella aerogenes, Salmonella typhimurium and Serratia marcescens.
J Gen Microbiol 1975 Mar
PMID:Reversible inactivation of the isocitrate dehydrogenase of Escherichia coli ML308 during growth on acetate. 109 97

We describe here the isolation of a mutant derivative of the drug resistance factor R1 (Meynell and Datta, 1966) that carries a nonsense mutation in a gene determining resistance to penicillins. We have used this mutant R1 to isolate derivatives of Escherichia coli and Klebsiella pneumoniae that contain nonsense suppressors (Sup- strains) by screening penicillin-resistant revertants of strains containing the mutant R factor for the presence of such suppressors. This obviates the need to have known nonsense mutations in chromosomal genes. Theoretically, suppressor-containing derivatives of any bacterial species that can maintain and express R1 can be constructed.
Mol Gen Genet 1975 Jul 10
PMID:A method for isolating nonsense suppressors in enterobacteriaceae using an amber mutant of the drug resistance factor R1. 109 92

A 6940 bp Klebsiella pneumoniae chromosomal DNA fragment, containing genes involved in pyrroloquinoline quinone (PQQ) biosynthesis, was sequenced. Six open reading frames, pqqA, pqqB, pqqC, pqqD, pqqE and pqqF were identified in the pqq operon, which coded for polypeptides of 2764 (23 amino acids), 33,464, 28,986, 10,436, 42,881 and 83,616 Da, respectively. The transcription startpoint was mapped by primer extension analysis, upstream of pqqA, and promoter boxes could be identified. The gene products of pqqB, pqqC, pqqE and pqqF were detected in maxi-cells and the molecular weights of the proteins corresponded with the molecular weights deduced from the nucleotide sequence. The gene products of pqqA, pqqB, pqqC, pqqD and pqqE show 49%-64% identity in amino acid sequence with those of pqqIV, pqqV, pqqI, pqqII and pqqIII respectively in the cloned pqq cluster of Acinetobacter calcoaceticus. The 84 kDa protein encoded by pqqF, which is not present in the cloned pqq cluster of A. calcoaceticus but which is essential for PQQ biosynthesis in K. pneumoniae and Escherichia coli, seems to belong to a family of proteases.
Mol Gen Genet 1992 Mar
PMID:Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon. 131 37

The genes xylA and xylB were cloned together with their promoter region from the chromosome of Klebsiella pneumoniae var. aerogenes 1033 and the DNA sequence (3225 bp) was determined. The gene xylA encodes the enzyme xylose isomerase (XI or XylA) consisting of 440 amino acids (calculated M(r) of 49,793). The gene xylB encodes the enzyme xylulokinase (XK or XylB) with a calculated M(r) of 51,783 (483 amino acids). The two genes successfully complemented xyl mutants of Escherichia coli K12, but no gene dosage effect was detected. E. coli wild-type cells which harbored plasmids with the intact xylAKp 5' upstream region in high copy number (but lacking an active xylB gene on the plasmids) were phenotypically xylose-negative and xylose isomerase and xylulokinase activities were drastically diminished. Deletion of 5' upstream regions of xylA on these plasmids and their substitution by a lac promoter resulted in a xylose-positive phenotype. This also resulted in overproduction of plasmid-encoded xylose isomerase and xylulokinase activities in recombinant E. coli cells.
Mol Gen Genet 1992 Aug
PMID:Cloning and expression of the genes for xylose isomerase and xylulokinase from Klebsiella pneumoniae 1033 in Escherichia coli K12. 132 98

The cloning and sequence determination is reported of the DNA region of Rhizobium leguminosarum coding for glutamine synthetase II (GSII). An open reading frame (ORF) encoding 326 amino acids was defined as the glnII gene on the basis of its similarity to other glnII genes and the ability of a DNA fragment carrying this ORF to complement the glutamine auxotrophy of a Klebsiella pneumoniae glnA mutant. We find that the glnII gene in R. leguminosarum is transcribed as a monocistronic unit from a single promoter, which shows structural features characteristic of rpoN (ntrA)-dependent promoters. In K. pneumoniae, such promoters require the ntrC and rpoN (ntrA) gene products for transcription. The intracellular level of glnII mRNA changes when R. leguminosarum is grown on different nitrogen sources, as expected for regulation by the nitrogen regulatory system. Promoter deletion analysis has shown that an extensive upstream DNA sequence (316 bp) is essential for in vivo activation of the glnII promoter in different biovars of R. leguminosarum. This DNA region requires a wild-type ntrC gene for activity and includes two conserved putative NtrC-binding site sequences. The results conclusively show that transcription from the R. leguminosarum glnII promoter is fully dependent on positive control by NtrC protein and on an upstream activator sequence (UAS).
Mol Gen Genet 1992 Sep
PMID:Activation of the Rhizobium leguminosarum glnII gene by NtrC is dependent on upstream DNA sequences. 135 39

A low-molecular-mass cytotoxin produced by Klebsiella oxytoca isolated previously from patients with antibiotic-associated haemorrhagic enterocolitis was purified, and its biological and chemical properties were elucidated. The toxin inhibited the syntheses of DNA and RNA by HEp-2 cells dose-dependently, whereas protein synthesis was only slightly inhibited, as measured by the incorporation of radioactive precursors. When synchronously cultured HEp-2 cells were examined in the presence of cytotoxin, inhibition of DNA synthesis occurred promptly within 5 h, but cell-rounding, the earliest visible morphological change, was not observed until 6 h after exposure. The intracellular levels of ATP decreased with an approximately similar time course. These results suggest that cytotoxicity toward HEp-2 cells is primarily due to the inhibitory effect of the cytotoxin on nucleic acid synthesis, possibly on DNA synthesis. Cell rounding and cell death were induced even in the absence of the cytotoxin after incubation with the cytotoxin for 6 h. The cytotoxin was heat-labile, cytotoxic activity decreasing to 50% of the initial level on heating at 70 degrees C for 20 min. Plasmids were extracted from three strains of K. oxytoca producing the cytotoxin and analysed by agarose gel electrophoresis. Two strains possessed plasmids of different sizes, but one strain possessed no plasmid, indicating that the cytotoxin is probably chromosomally encoded. Analysis by NMR and FAB-mass-spectrometry revealed that the molecular mass of the cytotoxin should be 217.1062 Da (exact mass), its molecular formula being C8H15O4N3.
J Gen Microbiol 1992 Sep
PMID:Biological activities and chemical composition of a cytotoxin of Klebsiella oxytoca. 140 92

The expression under microaerobic conditions of the Rhizobium meliloti nifA and consequently the nifHDK genes was found to be negatively regulated by ammonia and nitrate. Assimilation of the ammonia to glutamate and glutamine is not required for this regulation to occur. This indicates that ammonia itself, and not a product of its metabolism, may be regulating nif expression. Unlike the situation in Klebsiella pneumoniae, NtrC is apparently not involved in mediating the ammonia effect on nifA expression in R. meliloti. Neither does the fixK gene product, which is known to regulate nifA in R. meliloti, appear to be involved in mediating the ammonia effect. The regulation of nifA by ammonia is shown to be mediated through the FixL protein. A truncated fixJ gene, the product of which has been shown to induce nifA expression irrespective of the oxygen status of the cell, also circumvented the repressive effect of ammonia on nifA expression. This suggests that the ammonia effect is mediated through the FixLJ regulatory cascade. Interestingly no effect of ammonia on fixK expression was observed.
Mol Gen Genet 1992 Sep
PMID:Ammonia regulation of the Rhizobium meliloti nitrogenase structural and regulatory genes under free-living conditions: involvement of the fixL gene product? 140 87

A 1.95 kb DNA fragment containing the aly gene from Klebsiella pneumoniae, which encodes an alginate lyase, has been ligated into the broad-host-range vector pLAFR3. Transfer of the resultant recombinant plasmid, pALY8, into mucoid and non-mucoid strains of Pseudomonas aeruginosa resulted in expression of the alginate lyase. The heterologously expressed alginate lyase, which had the same isoelectric point and substrate specificity as the native enzyme, altered the morphology of mucoid strains. Analysis of the extracellular material from mucoid strains revealed that lyase expression reduced the M(r) and overall yield of alginate produced. The mature form of the recombinant enzyme was the same as that produced extracellularly by Klebsiella pneumoniae; however, most of the alginate lyase was retained intracellularly by P. aeruginosa.
J Gen Microbiol 1992 Aug
PMID:Heterologous expression of an alginate lyase gene in mucoid and non-mucoid strains of Pseudomonas aeruginosa. 152 6

We have determined the sequence of the lamB gene from Klebsiella pneumoniae. It encodes the precursor to the LamB protein, a 429 amino acid polypeptide with maltoporin function. Comparison with the Escherichia coli LamB protein reveals a high degree of homology, with 325 residues strictly identical. The N-terminal third of the protein is the most conserved part of the molecule (1 change in the signal sequence, and 13 changes up to residue 146 of the mature protein). Differences between the two mature proteins are clustered mainly in six regions comprising residues 145-167, 173-187, 197-226, 237-300, 311-329, and 367-387 (K. pneumoniae LamB sequence). The most important changes were found in regions predicted by the two-dimensional model of LamB folding to form loops on the cell surface. In vivo maltose and maltodextrin transport properties of E. coli K12 and K. pneumoniae strains were identical. However, none of the E. coli K12 LamB-specific phages was able to plaque onto K. pneumoniae. Native K. pneumoniae LamB protein forms highly stable trimers. The protein could be purified by affinity chromatography on starch-Sepharose as efficiently as the E. coli K12 LamB protein, indicating a conservation of the binding site for dextrins. However, none of the monoclonal antibodies directed against native E. coli K12 LamB protein recognized native purified K. pneumoniae LamB protein. These data indicate that most of the variability occurs within exposed regions of the protein and provide additional support for the proposed model of LamB folding.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Gen Genet 1992 Jun
PMID:DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: implications for the topology and the pore functions in maltoporin. 153 83

A trivalent lanthanide ion, erbium (Er3+), has been used in combination with a magnetic separation technique to isolate seven bacterial species from suspensions in 0.9% saline. Erbium has an exceptionally high atomic magnetic moment of 9.3 Bohr magnetons, and following addition as ErCl3 (final concentration 5 mM) to bacterial suspensions, it imparts the magnetic moment to the bacterial cells by ionic binding to the cell surface. Strains of Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis, Pseudomonas aeruginosa, Staphylococcus epidermidis, Staphylococcus saprophyticus and Enterococcus faecalis were obtained from the Quality Control Depository of The Cleveland Clinic Foundation, Cleveland, Ohio, USA as suspensions in 0.9% NaCl, in concentrations ranging from 10(2) to 10(8) c.f.u. ml-1. Bacteria were separated from solution inside a capillary flow cell exposed to a highly non-homogeneous magnetic field (maximum field intensity was 0.4 T) and quantified by a light scattering method. The quantity of cellular deposition in the magnetic field was correlated with the initial concentration of cells in the suspension, expressed in c.f.u. ml-1, and sample volume (1.5 and 3.0 ml), sample pH (prior to ErCl3 addition), affinity to Gram stain (negative vs positive) and species.(ABSTRACT TRUNCATED AT 250 WORDS)
J Gen Microbiol 1992 Jan
PMID:Quantitative separation of bacteria in saline solution using lanthanide Er(III) and a magnetic field. 155 57


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