Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.3.1.28 (chloramphenicol acetyltransferase)
5,100 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A promoterless chloramphenicol acetyltransferase gene (cat) was used to construct recA-cat operon fusions to quantitatively examine the transcriptional regulation of the Pseudomonas aeruginosa recA gene in P. aeruginosa PAO. Wild-type P. aeruginosa containing the recA8-cat fusion was treated with methyl methanesulfonate (MMS) and showed immediate induction of chloramphenicol acetyltransferase (CAT) specific activity, whereas a recA::Tn501 mutant of P. aeruginosa containing recA8-cat showed no induction with MMS. This indicated that a functional copy of recA was required for derepression of recA transcription and that P. aeruginosa recA protein was a positive regulatory factor promoting its own expression. Compared with that in the wild type, the uninduced level of CAT in recA8-cat-containing cells was reduced by approximately one-half in the recA::Tn501 mutant, indicating that recA+-dependent spontaneous induction contributes to the uninduced levels of recA expression in P. aeruginosa. MMS (0.012%) caused recA-directed CAT synthesis to increase almost immediately, with maximum CAT activity, fourfold higher than uninduced levels, attained at 60 min postinduction. The kinetics of recA8-cat fusion activity were shown to be directly related to the MMS doses used. Another fusion called recAa1-cat, where cat was located between the two transcriptional terminators of the P. aeruginosa recA gene, also showed dose-dependent induction by MMS, but the CAT activity from recAa1-cat was only one-half of that obtained with recA8-cat under the same conditions. Treatment of recA+ P. aeruginosa containing recA8-cat with UV irradiation produced an immediate effect on recA8-cat transcription and showed little UV dose dependency at doses of 5 J/m2 or greater. Treatment with 10 J/m2 produced peak levels of recA-directed CAT activity, fivefold higher than background levels, by 60 min postirradiation; CAT activity remained at peak levels during the 120 min of the experiment. In contrast, nalidixic acid had a weak effect on recA8-cat expression in P. aeruginosa, although the response was dose dependent. Nalidixic acid (800 micrograms/ml) produced maximal CAT activity that was only twofold higher than background levels.
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PMID:Autogenous regulation and kinetics of induction of Pseudomonas aeruginosa recA transcription as analyzed with operon fusions. 313 34

We isolated a new transposon, Tn2001, from the group P-2 plasmid Rms159-1 in Pseudomonas aeruginosa. Tn2001-encoded chloramphenicol resistance did not result from the formation of chloramphenicol acetyltransferase. Tn2001 was transposable between temperate phages and conjugative and nonconjugative plasmids belonging to various incompatibility groups, including P-1, P-3, P-4, P-5, P-7, and P-8 in P. aeruginosa. Transposition occurred independently of the general recombination ability of the Pseudomonas host, and its frequency varied between 10(-1) and 10(-8), depending upon the donor and recipient replicons. Tn2001 transposition also occurred in a recombination-deficient strain of Escherichia coli. Agarose gel electrophoresis and electron microscopic observations revealed that Tn2001 could transpose to different sites in the RP4 replicon and that the transposed deoxyribonucleic acid fragment was 2.1 kilobases long.
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PMID:Tn2001, a transposon encoding chloramphenicol resistance in Pseudomonas aeruginosa. 626 Jul 39

The mechanisms of resistance encountered in bacteria causing infection in the patient at risk for infection are diverse. Most resistance currently seen is the result of plasmid transfer rather than mutational events. However, extensive use of antimicrobial agents in the hospital has caused the selection of organisms resistant to many agents by virtue of chromosomally mediated mechanisms. Staphylococcus aureus resistant to beta-lactams due to altered penicillin-binding proteins has become a problem in certain patients such as narcotic addicts and chronic care facility patients exposed to many beta-lactam antibiotics. S. epidermidis has also proved to be a problem in patients with indwelling foreign devices, and altered penicillin-binding proteins also make these organisms resistant to available penicillins and cephalosporins. Streptococcus fecalis has become increasingly resistant to aminoglycosides, erythromycin, and tetracyclines due to plasmid-mediated enzymes. Hemophilus influenzae resistant to both penicillins and chloramphenicol by virtue of beta-lactamases and chloramphenicol transacetylase has been encountered. Beta-lactamase-mediated resistance of Enterobacteriaceae, Escherichia coli, and Klebsiella pneumoniae to beta-lactam antibiotics has increased, and resistance of Serratia marcescens and Pseudomonas aeruginosa to aminoglycosides and penicillins is a widespread phenomenon. Mechanisms to reduce resistance will include not only careful attention to hygienic practices but also more appropriate use of antibiotics selecting the proper agent depending on the type of patient and environment in which the infection develops.
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PMID:Current mechanisms of resistance to antimicrobial agents in microorganisms causing infection in the patient at risk for infection. 637 59

The in vitro activity of three fluorine analogs of chloramphenicol in which the hydroxyl group at position 3 had been replaced with a fluorine was compared with that of chloramphenicol and thiamphenicol. Compound SCH 24893 was the most active agent against staphylococci and Bacteroides strains, and compound SCH 25298 was the most active against Haemophilus, Neisseria, enterococcus, and Klebsiella strains. Serratia marcescens and Pseudomonas aeruginosa strains resistant to chloramphenicol were resistant to the compounds. The agents inhibited all of the Shigella, Salmonella, Staphylococcus aureus, and enterococcus strains resistant to chloramphenicol. They inhibited most (82%) of Escherichia coli and half of the Klebsiella pneumoniae strains which were resistant to chloramphenicol. Isolates in which resistance to chloramphenicol was shown to be plasmic mediated and due to chloramphenicol transacetylase were inhibited by all three agents.
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PMID:In vitro activity of chloramphenicol and thiamphenicol analogs. 744 8

The multidrug resistance plasmid pBWH301 was shown to contain a sull-associated integron with five inserted gene cassettes, aacA7-catB3-aadB-oxa2-orfD, all of which can be mobilized by the integron-encoded DNA integrase. The aadB, oxa2, and orfD cassettes are identical to known cassettes. The aacA7 gene encodes a protein that is a member of one of the three known families of aminoglycoside acetyltransferases classified as AAC(6')-I. The chloramphenicol acetyltransferase encoded by the catB3 gene is closely related to members of a recently identified family of chloramphenicol acetyltransferases. The catB3 gene displays a relatively high degree of sequence identity to a chromosomally located open reading frame in Pseudomonas aeruginosa, and this may represent evidence for the acquisition by a cassette of a chromosomal gene.
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PMID:New mobile gene cassettes containing an aminoglycoside resistance gene, aacA7, and a chloramphenicol resistance gene, catB3, in an integron in pBWH301. 779 74

The disulfide loop domain of Pseudomonas aeruginosa PAO pilin was altered by insertion of a chloramphenicol acetyltransferase gene into the pilin gene so that the C-terminal nine amino acids were replaced with 11 new amino acids. The altered pilin gene was transferred into wild-type PAO by recombination, where it did not affect normal piliation as observed by transmission electron microscopy or change of sensitivity to f116, PO4, B9, and Pf1 pilus-specific bacteriophages. However, the binding to human pneumocyte A549 cells was markedly reduced when tested in an in vitro binding assay (2 to 6 bacteria bound per A549 cell for the mutant bacteria compared with 50 bacteria per A549 cell for the wild-type bacteria). Additionally, when susceptible A.BY/SnJ mice were challenged with wild-type P. aeruginosa PAO and with P. aeruginosa PAO-MP (altered pilin gene), a 50% lethal dose of 3 x 10(6) bacteria per mouse was observed for PAO-MP compared with 7 x 10(4) bacteria per mouse for PAO. Approximately 90 of the adherence capability of P. aeruginosa PAO is seemingly attributable to the C-terminal disulfide loop adherence domain of pili. The pilus adherence function contributes significantly to the virulence of P. aeruginosa PAO in the A.BY/SnJ mouse infection model.
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PMID:Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in mice. 792 65

The transcriptional organization of the exoenzyme S trans-regulatory locus was studied by using promoter fusion and transcriptional start site mapping analyses. The 5' regions flanking open reading frames encoding ExsC, ExsB, ExsA, and ExsD were cloned in both orientations into the promoter vector pQF26, which contains the chloramphenicol acetyltransferase reporter gene (cat). CAT activity from each promoter fusion transformed into Pseudomonas aeruginosa and Escherichia coli was measured. The trans-regulatory locus promoters demonstrated low to undetectable CAT activity in E. coli regardless of the orientation of the DNA fragment relative to the reporter gene. In P. aeruginosa two of the promoter clones containing DNA located 5' of exsC (pC) and exsD (pD) demonstrated significant CAT activity. Transcriptional initiation from pC and pD was dependent on the orientation of the DNA fragment, the inclusion of a chelator in the growth medium, and the presence of a functional exsA gene. Transcriptional start sites were mapped for the pC and pD promoter regions by using total RNA isolated from P. aeruginosa strains grown in medium including a chelator. Our data are consistent with an operon model for the transcriptional organization of the exoenzyme S trans-regulatory locus. In addition, ExsA appears to be involved in controlling transcriptional initiation from both the trans-regulatory locus and a region located immediately downstream of the exsA gene.
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PMID:Transcriptional organization of the trans-regulatory locus which controls exoenzyme S synthesis in Pseudomonas aeruginosa. 802 Nov 64

A 1954-bp DNA fragment containing the blaMOX-1 gene, identified on a large resident plasmid (pRMOX-1) of Klebsiella pneumoniae NU2936, was sequenced and an open reading frame (ORF) coding for a 390-amino-acid (aa) MOX-1 was found. The total deduced aa sequence of MOX-1 shared considerable homology with that of AmpC-type class C beta-lactamases of Gram- bacteria, especially of Pseudomonas aeruginosa PAO1 [51.3%; 63.8% at the nucleotide (nt) level]. However, the regulatory gene ampR and a 38-bp AmpR-binding region were not present upstream from blaMOX-1, although the expression of P. aeruginosa ampC is directly regulated by AmpR. Possible -35 and -10 regions, a Shine-Dalgarno (SD) sequence and terminators were identified which are peculiar to blaMOX-1. On the other hand, a sequence highly homologous (91.6%) to the region upstream from dhfrX in the In7 integron carried by plasmid pDGO100 was found upstream from blaMOX-1 at nt 1 to 488. No significant difference was detected between the promoter activities of blaMOX-1 in ampD- and ampD+ strains of Enterobacter cloacae, as measured by the chloramphenicol acetyltransferase (CAT) assay. These results clearly show that blaMOX-1 belongs to the group of ampC-related bla genes and that it is expressed constitutively, independently of transcriptional regulators such as AmpR, AmpG and AmpD. Homology analysis among AmpC enzymes or ampC genes implied that integration of the chromosomal ampC gene into a large resident plasmid, followed by transconjugation, was involved in the evolution of blaMOX-1.
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PMID:Characterization of a plasmid-borne and constitutively expressed blaMOX-1 gene encoding AmpC-type beta-lactamase. 811 96

In Pseudomonas aeruginosa, production of exotoxin A, an ADP-ribosyltransferase, is a complex and highly regulated process. Two positively acting regulatory genes, regA and regB, have been cloned and characterized. To identify additional exotoxin A regulatory genes, we have characterized four N-methyl-N'-nitro-N-nitrosoguanidine-generated mutants of P. aeruginosa PA103 which are deficient in exotoxin A production. These mutants (PA103-8, PA103-15, PA103-16, and PA103-19) do not accumulate intracellular exotoxin A and are not complemented by the cloned toxA or regAB genes. This observation indicates that the lesion(s) in the mutants is probably in an exotoxin A regulatory gene(s) and is not in the genes for secretion of exotoxin A or in the toxA or regAB genes. To assess the effect of the putative regulatory mutations on the toxA and regAB genes, we compared the activity of the toxA and regAB promoters in the mutant and parental strains using plasmids containing the genes for beta-galactosidase or chloramphenicol acetyltransferase under the control of either the toxA or the regAB promoter. The toxA promoter-beta-galactosidase fusion plasmid could not be maintained in PA103-8. beta-Galactosidase expression driven by the toxA promoter was absent in the mutant PA103-19 and occurred at a low level, which was not repressed by iron in mutants PA103-15 and PA103-16. The regAB genes are temporally controlled by two promoters, P1 and P2. In all four mutants, regAB P1 promoter activity was reduced; however, expression under the control of the regAB P2 promoter was normal. These observations suggest the existence of one or more regulatory genes which directly affect expression of both the toxA and the regAB P1 promoters.
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PMID:Characterization of Pseudomonas aeruginosa mutants that are deficient in exotoxin A synthesis and are altered in expression of regA, a positive regulator of exotoxin A. 811 61

Enterococcus faecium BM4145, a clinical isolate from urine, was resistant to streptogramin group A antibiotics by inactivation. The strain harbored a plasmid containing a gene, satA, responsible for this resistance; this gene was cloned and sequenced. It encoded SatA, a protein deduced to be 23,634 Da in mass and homologous with a new family of chloramphenicol acetyltransferases described in Agrobacterium tumefaciens, Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. The similarity of SatA to other acetyltransferases, LacA (thiogalactoside acetyltransferase) and CysE (serine acetyltransferase) from E. coli, and to two putative acetyltransferases, NodL from Rhizobium leguminosarum and Urf1 from E. coli, was also observed in a region considered to be the enzyme's active site. Acetylation experiments indicated that acetyl coenzyme A was necessary for SatA activity and that a single acetylated derivative of pristinamycin IIA was produced. Other members of the streptogramin A group such as virginiamycin M and RP54476 were also substrates for the enzyme. We conclude that resistance to the streptogramin A group of antibiotics in E. faecium BM4145 is due to acetylation by an enzyme related to the novel chloramphenicol acetyltransferase family.
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PMID:Identification of the satA gene encoding a streptogramin A acetyltransferase in Enterococcus faecium BM4145. 825 33


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