568 results on '"F Rojo"'
Search Results
552. Identification of the sequences recognized by phage phi 29 transcriptional activator: possible interaction between the activator and the RNA polymerase.
- Author
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Nuez B, Rojo F, Barthelemy I, and Salas M
- Subjects
- Bacillus subtilis, Bacteriophages enzymology, Base Sequence, Chromosome Deletion, DNA, Viral metabolism, Deoxyribonuclease I, Molecular Sequence Data, Mutagenesis, Promoter Regions, Genetic, Bacteriophages genetics, DNA-Directed RNA Polymerases metabolism, Transcription Factors metabolism, Viral Proteins
- Abstract
Expression of Bacillus subtilis phage phi 29 late genes requires the transcriptional activator protein p4. This activator binds to a region of the late A3 promoter spanning nucleotides -56 to -102 relative to the transcription start site, generating a strong bending Tin the DNA. In this work the target sequences recognized by protein p4 in the phage phi 29 late A3 promoter have been characterized. The binding of protein p4 to derivatives of the late A3 promoter harbouring deletions in the protein p4 binding site has been studied. When protein p4 recognition sequences were altered, the activator could only bind to the promoter in the presence of RNA polymerase. This strong cooperativity in the binding of protein p4 and RNA polymerase to the promoter suggests the presence of direct protein-protein contacts between them.
- Published
- 1991
- Full Text
- View/download PDF
553. Short N-terminal deletions in the phage phi 29 transcriptional activator protein impair its DNA-binding ability.
- Author
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Rojo F and Salas M
- Subjects
- Amino Acid Sequence, Bacillus subtilis genetics, DNA Fingerprinting, DNA-Binding Proteins genetics, Electrophoresis, Polyacrylamide Gel, Genes, Bacterial, Genes, Viral, Molecular Sequence Data, Mutation, Promoter Regions, Genetic, Bacteriophages genetics, Chromosome Deletion, DNA, Viral genetics, DNA-Binding Proteins metabolism, Transcriptional Activation, Viral Proteins genetics
- Abstract
The expression of Bacillus subtilis phage phi 29 late genes from the A3 promoter requires the viral protein p4. This protein is a transcriptional activator which binds to a region of the A3 promoter located between nucleotides -56 to -102, relative to the transcription start point. Mutants at the N terminus of protein p4 have been constructed and their function investigated. The binding of these deletion mutants to the late A3 promoter has been analyzed by gel retardation and DNase I footprinting assays. The results indicate that the N terminus of protein p4 could be involved in its binding to the A3 promoter, suggesting that it may not be a typical Cro-like helix-turn-helix DNA-binding protein.
- Published
- 1990
- Full Text
- View/download PDF
554. Cloning and expression of the ponB gene, encoding penicillin-binding protein 1B of Escherichia coli, in heterologous systems.
- Author
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Plá J, Rojo F, de Pedro MA, and Ayala JA
- Subjects
- Ampicillin metabolism, Carrier Proteins isolation & purification, Carrier Proteins metabolism, Cell Membrane metabolism, Cell Membrane ultrastructure, Cloning, Molecular, Gene Expression, Genotype, Kinetics, Microscopy, Electron, Muramoylpentapeptide Carboxypeptidase isolation & purification, Muramoylpentapeptide Carboxypeptidase metabolism, Penicillin-Binding Proteins, Penicillins metabolism, Plasmids, Pseudomonas genetics, Restriction Mapping, Salmonella typhimurium genetics, Bacterial Proteins, Carrier Proteins genetics, Escherichia coli genetics, Genes, Bacterial, Hexosyltransferases, Muramoylpentapeptide Carboxypeptidase genetics, Peptidyl Transferases
- Abstract
A fragment from the ponB region of the Escherichia coli chromosome comprising the promoterless sequence encoding penicillin-binding protein 1B (PBP 1B) has been cloned in a broad-host-range expression vector under the control of the kanamycin resistance gene promoter present in the vector. The hybrid plasmid (pJP3) was used to transform appropriate strains of Salmonella typhimurium, Pseudomonas putida, and Pseudomonas aeruginosa. In all instances, the coding sequence was expressed in the heterologous hosts, yielding a product with electrophoretic mobility, protease accessibility, membrane location, and beta-lactam-binding properties identical to those of native PBP 1B in E. coli. These results indicated that PBP 1B of E. coli is compatible with the cytoplasmic membrane environment of unrelated bacterial species and support the idea that interspecific transfer of mutated alleles of genes coding for PBPs could potentially be an efficient spreading mechanism for intrinsic resistance to beta-lactams.
- Published
- 1990
- Full Text
- View/download PDF
555. A family of positive regulators related to the Pseudomonas putida TOL plasmid XylS and the Escherichia coli AraC activators.
- Author
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Ramos JL, Rojo F, Zhou L, and Timmis KN
- Subjects
- Amino Acid Sequence, AraC Transcription Factor, Erwinia genetics, Escherichia coli Proteins, Molecular Sequence Data, Sequence Homology, Nucleic Acid, Transcription, Genetic, Bacterial Proteins, Escherichia coli genetics, Plasmids, Pseudomonas genetics, Repressor Proteins genetics, Transcription Factors genetics, Transcription Factors metabolism
- Abstract
The XylS family consists of a least 8 different transcriptional regulators. Six of these proteins are positive regulators for the catabolism of carbon sources (benzoate and sugars) in Escherichia coli, Pseudomonas putida and Erwinia carotovora, and two of them are involved in pathogenesis in Escherichia coli and Yersinia enterocolitica. Based on protein alignments, the members of this family exhibit a long stretch of homology at the C-terminal end. The regulators involved in the catabolism of carbon sources stimulate transcription from their respectively regulated promoters only in the presence of effectors. In two of the regulators, mutations at the non-homologous N-terminus alter affinity and specificity for effectors while mutations at the conserved C-terminus part decrease activation of transcription from their corresponding regulated promoters. It is thus probable that the variable N-terminus end in this family of regulators contains the motif involved in effector recognition, while the C-terminal end is involved in DNA-binding. These proteins seem to be related by common ancestry and may act through similar mechanisms of positive regulation effected through similar folding patterns.
- Published
- 1990
- Full Text
- View/download PDF
556. Bend induced by the phage phi 29 transcriptional activator in the viral late promoter is required for activation.
- Author
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Rojo F, Zaballos A, and Salas M
- Subjects
- Amino Acid Sequence, Base Sequence, Chromosome Deletion, Deoxyribonuclease I, Genes, Viral, Models, Molecular, Molecular Sequence Data, Mutation, Nucleotide Mapping, Plasmids, Protein Binding, Trans-Activators genetics, Bacillus subtilis genetics, Bacteriophages genetics, DNA, Viral genetics, Nucleic Acid Conformation, Promoter Regions, Genetic, Trans-Activators metabolism, Transcription, Genetic
- Abstract
Transcription initiation from the Bacillus subtilis phage phi 29 late A3 promoter requires the viral protein p4, a transcriptional activator. Protein p4 binds to a region of the A3 promoter, located between nucleotides -50 and -100 relative to the transcription start site, that presents a sequence-directed curvature. This curvature is enhanced when protein p4 binds to the promoter. A number of deletion mutants at the carboxyl end of protein p4 have been constructed and their behavior as transcriptional activators of the late A3 promoter has been investigated. The binding of these deletion mutants to the late A3 promoter has been analyzed by gel retardation, DNase I footprinting, methylation interference and circular permutation assays. The results suggest that the last 12 amino acid residues of protein p4, six of which are positively charged, although not involved in the specific recognition of the promoter are responsible for part of the bend induced by protein p4 in its binding site. Evidence is presented which suggests that full induction of this curvature is needed for the transcription activation process. A model is proposed for protein p4 interaction with the A3 promoter, in which the bend is induced in two steps: first, two monomers of protein p4 bind to the inverted recognition sequences, subsequent interaction between them generating a bend between these sequences; second, the highly basic carboxyl terminus of protein p4 establishes non-specific electrostatic interactions with the DNA backbone inducing a bend at both ends of the protein p4 binding region.
- Published
- 1990
- Full Text
- View/download PDF
557. Signal-regulator interactions. Genetic analysis of the effector binding site of xylS, the benzoate-activated positive regulator of Pseudomonas TOL plasmid meta-cleavage pathway operon.
- Author
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Ramos JL, Michan C, Rojo F, Dwyer D, and Timmis K
- Subjects
- Amino Acid Sequence, AraC Transcription Factor, Base Sequence, Benzoates metabolism, Codon genetics, Escherichia coli genetics, Escherichia coli Proteins, Kinetics, Molecular Sequence Data, Mutation, Sequence Homology, Nucleic Acid, Transcription, Genetic, Bacterial Proteins, Benzoates pharmacology, Gene Expression Regulation, Bacterial drug effects, Genes, Bacterial drug effects, Genes, Regulator, Operon, Plasmids, Pseudomonas genetics, Repressor Proteins genetics, Transcription Factors genetics
- Abstract
This study reports a genetic analysis of the interactions between a positive regulator of gene expression and its effector molecules. Transcription of the TOL plasmid meta-cleavage pathway operon is specifically stimulated by the XylS protein positive regulator either through activation of this regulator by benzoate effectors or through its hyperproduction. One xylS mutant that exhibits constitutive expression of the operon promoter has been characterized, together with six mutants encoding altered XylS proteins that recognize as effectors benzoate analogues that are non-effectors for the XylS wild-type protein. The changes in two mutant regulators are located at the N-terminal end of the protein, within a putative beta-pleated domain. These mutant proteins exhibit a markedly increased affinity for normal benzoate effectors, with K's values fivefold to 60-fold lower than those of the wild-type XylS protein. They are additionally activated by new effectors having certain substituents at position 2, 3 and 4 of the aromatic ring. Two other mutant proteins recognize new effectors having substituents at position 4 and 5 of the aromatic ring, and contain mutations at their C-terminal end within a putative alpha-helix-rich domain. Three other mutations, one of which leads to constitutive expression from Pm, each result in an amino acid change in the central region of the regulator. These findings suggest but do not prove that the effector binding pocket of the XylS protein may be composed of two or more non-contiguous segments of its primary structure. The XylS protein exhibits homology with the AraC protein of Escherichia coli, a protein that stimulates transcription from ara promoters when it is activated by arabinose or benzoate. Mutations influencing effector activation of the XylS protein characterized in this study are all located in regions exhibiting a high degree of homology with the corresponding aligned sequence of AraC protein.
- Published
- 1990
- Full Text
- View/download PDF
558. Scanning electron microscope study of mature and immature worms of a Sanguinicola sp. (Digenea: Sanguinicolidae).
- Author
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Simon-Martin F and Rojo-Vazquez F
- Subjects
- Aging, Animals, Microscopy, Electron, Scanning, Spain, Cyprinidae parasitology, Schistosomatidae ultrastructure
- Abstract
A study was made of the morphological details of the tegument of mature (40-42 days) and immature (28 days) Sanguinicola sp. found in cyprinids of certain rivers of the province of Salamanca (Spain). In the adult worms, the entire tegument was covered with microvilli; the parasite showed various kinds of sensory organs, whose distribution is specified here. The lateral margins revealed strong denticules (except the anterior and posterior extremities) with spines and bristles. The immature worms showed a far simpler external structure; they lacked microvilli but did show orifices which could be sensory organelles. The lateral margins only showed the presence of spines.
- Published
- 1984
- Full Text
- View/download PDF
559. Binding of 125I-labeled beta-lactam antibiotics to the penicillin binding proteins of Escherichia coli.
- Author
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Rojo F, Ayala JA, de la Rosa EJ, de Pedro MA, Arán V, Berenguer J, and Vázquez D
- Subjects
- Ampicillin metabolism, Anti-Bacterial Agents pharmacology, Binding, Competitive, Escherichia coli metabolism, Iodine Radioisotopes, Kinetics, Penicillin-Binding Proteins, Structure-Activity Relationship, Anti-Bacterial Agents metabolism, Bacterial Proteins, Carboxypeptidases metabolism, Carrier Proteins metabolism, Escherichia coli Proteins, Hexosyltransferases, Muramoylpentapeptide Carboxypeptidase metabolism, Penicillins metabolism, Peptidoglycan Glycosyltransferase, Peptidyl Transferases, Serine-Type D-Ala-D-Ala Carboxypeptidase
- Abstract
125I-Labeled derivatives of the beta-lactam antibiotics cephalexin, cephradine, cefaclor and 6-alpha-aminopenicillanic acid have been obtained by reacting these compounds with (125I)-Bolton-Hunter reagent. The following target proteins were found in Escherichia coli: (1) The derivatives of cephalexin, cefaclor and cephradine preferentially interact with the high molecular weight penicillin binding proteins ( PBP1a and PBP1b ); (2) The 125I- derivative of 6-alpha-aminopenicillanic acid is preferentially bound by the low molecular weight penicillin binding proteins 4 and 5/6. The iodinated derivatives showed a very high affinity of binding to their target proteins with apparent half-saturating concentrations in the nano -molar range.
- Published
- 1984
- Full Text
- View/download PDF
560. Assemblage of ortho cleavage route for simultaneous degradation of chloro- and methylaromatics.
- Author
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Rojo F, Pieper DH, Engesser KH, Knackmuss HJ, and Timmis KN
- Subjects
- Alcaligenes enzymology, Alcaligenes genetics, Bacterial Proteins genetics, Gene Expression Regulation, Genetic Engineering, Isomerases genetics, Isomerases metabolism, Mixed Function Oxygenases genetics, Mixed Function Oxygenases metabolism, Oxidoreductases genetics, Oxidoreductases metabolism, Oxygenases genetics, Oxygenases metabolism, Pseudomonas enzymology, Pseudomonas genetics, Bacterial Proteins metabolism, Benzoates metabolism, Biodegradation, Environmental, Chlorobenzoates metabolism, Genes, Bacterial, Intramolecular Transferases, Recombinant Proteins metabolism
- Abstract
Genetic engineering is a powerful means of accelerating the evolution of new biological activities and has considerable potential for constructing microorganisms that can degrade environmental pollutants. Critical enzymes from five different catabolic pathways of three distinct soil bacteria have been combined in patchwork fashion into a functional ortho cleavage route for the degradation of methylphenols and methylbenzoates. The new bacterium thereby evolved was able to degrade and grow on mixtures of chloro- and methylaromatics that were toxic even for the bacteria that could degrade the individual components of the mixtures. Except for one enzymatic step, the pathway was fully regulated and its component enzymes were only synthesized in response to the presence of pathway substrates.
- Published
- 1987
- Full Text
- View/download PDF
561. Fate of genetically-engineered bacteria in activated sludge microcosms.
- Author
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Dwyer DF, Hooper SW, Rojo F, and Timmis KN
- Subjects
- Biodegradation, Environmental, Models, Biological, Pseudomonas metabolism, Bacteria genetics, Environmental Pollutants, Genetic Engineering, Soil Microbiology, Water Microbiology
- Abstract
The conclusions that can be derived from this study regarding the fate of the GEMs and their ability to degrade added pollutants are as follows: 1. Both GEMs were able to survive in the microcoms. Because Pseudomonas sp. B13 has been cultured for a long time in the laboratory, it was not expected to survive well in the microcosm. Surprisingly, it and the derivative GEMs persisted at a high population level of approximately 10(5) bacteria/ml. Pure culture studies had demonstrated an ability of FR1(pFRC20P) to readily degrade simultaneous mixtures of 3CB and 4MB. In the microcosms, however, the GEM did not perform as well as expected, particularly when confronted with a shock load of a 3CB and 4MB mixture. Thus, the microcosm studies may be of potential help for making predictions concerning environmental applications of GEMs. 2. Pseudomonas sp. B13 derivative strains FR1 and FR1(pFRC20P) were able to degrade low concentrations of substituted benzoates within the complex ecosystem of the activated sludge microcosm. A good deal of information concerning the degradation pathway for aromatics by Pseudomonas sp. B13 was already known. This allowed for the construction of the stable, regulated pathways for the degradation of substituted aromatic compounds in both GEMs and indicates that the construction of similar GEMs for the degradation of environmental pollutants is a promising experimental strategy. 3. There was not any demonstrable, adverse effect of GEM addition to the microbial population level in the microcosm. The GEMs were even able to function in a protective manner for the indigenous populations by buffering them against the adverse effects of addition of substituted benzoates. In contrast, for microcosms lacking GEM addition, a wash-out of the bacterial population in the microcosm occurred (data not shown). 4. Lateral transfer of new genetic information (xylXYZLS) from the GEM chromosome to indigenous microorganisms was not detected, whereas transfer of the hybrid, mobilizable pFRC20P carrying the gene for lactone isomerase did apparently occur. In this particular case, transfer may have been beneficial for the community as a whole if it increased the ecosystem's ability to cope with the presence of toxic pollutants. As more GEMs are constructed for specific biotechnological applications the diversity and complexity of microcosms used to study their fate and function will increase. The ability of such studies to predict a priori the fate of these microorganisms will help to develop strategies both to decrease the risks associated with introducing GEMs into the environment and to increase and regulate the capacity of GEMs to degrade toxic pollutants.(ABSTRACT TRUNCATED AT 400 WORDS)
- Published
- 1988
562. Analysis of the different molecular forms of penicillin-binding protein 1B in Escherichia coli ponB mutants lysogenized with specialized transducing lambda (ponB+) bacteriophages.
- Author
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Rojo F, Ayala JA, De Pedro MA, and Vázquez D
- Subjects
- DNA Restriction Enzymes metabolism, DNA, Bacterial analysis, Electrophoresis, Polyacrylamide Gel, Escherichia coli enzymology, Gene Expression Regulation, Hexosyltransferases genetics, Multienzyme Complexes genetics, Mutation, Penicillin-Binding Proteins, Peptidyl Transferases genetics, Acyltransferases analysis, Bacterial Proteins, Bacteriophage lambda genetics, Carrier Proteins, Escherichia coli genetics, Hexosyltransferases analysis, Lysogeny, Multienzyme Complexes analysis, Muramoylpentapeptide Carboxypeptidase, Peptidyl Transferases analysis
- Abstract
Penicillin-binding protein (pbp) 1b, the main DD-transpeptidase/transglycosylase of Escherichia coli, is normally present in the cell in three molecular forms alpha, beta and gamma, differentiated by their mobility in sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The three molecular forms are enzymatically active in vitro and their relative amounts are kept fairly constant in most labelling experiments with radioactive beta-lactam antibiotics. In this paper, we have analyzed the expression of ponB (mrcB), the structural gene for pbp 1b, and the relation among the three forms of pbp 1b in ponB strains lysogenyzed by lambda 540 (ponB+) recombinant bacteriophages. Our data indicate that ponB is transcribed anti-clockwise on the E. coli chromosome and suggest that pbp 1b alpha is the first membrane-bound form of pbp 1b able to bind labelled beta-lactams, and is the precursor of pbp 1b beta which is, in turn, the precursor of pbp 1 beta gamma.
- Published
- 1984
- Full Text
- View/download PDF
563. Laboratory engineering of bacteria designed to degrade pollutants.
- Author
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Timmis KN, Rojo F, Ramos JL, Krumme ML, and Dwyer DF
- Subjects
- Bacteria genetics, Biodegradation, Environmental, Plasmids, Bacteria metabolism, Environmental Pollutants, Genetic Engineering, Soil Microbiology, Water Microbiology
- Published
- 1988
564. Biological activities specified by antibiotic resistance plasmids.
- Author
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Timmis KN, Gonzalez-Carrero MI, Sekizaki T, and Rojo F
- Subjects
- Drug Resistance, Microbial, Anti-Bacterial Agents pharmacology, Plasmids
- Abstract
Bacteria can display resistance to a wide spectrum of noxious agents and environmental conditions, and these properties are often mediated by genes located on extrachromosomal DNA elements called plasmids. Replication, vertical and horizontal transmission and evolution of these elements are discussed, and examples of the genes responsible for the resistance phenotypes are given. Selective forces that drive the evolution of new combinations of bacterial properties of particular importance in clinical situations are analysed.
- Published
- 1986
- Full Text
- View/download PDF
565. Variability in the posttranslational processing of penicillin-binding protein 1b among different strains of Escherichia coli.
- Author
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Rojo F, Berenguer J, Ayala JA, and de Pedro MA
- Subjects
- Cell Membrane enzymology, Escherichia coli enzymology, Penicillin-Binding Proteins, Peptide Mapping, Plasmids, Species Specificity, Acyltransferases genetics, Bacterial Proteins, Carrier Proteins, Escherichia coli genetics, Hexosyltransferases genetics, Multienzyme Complexes genetics, Muramoylpentapeptide Carboxypeptidase, Peptidyl Transferases genetics, Protein Processing, Post-Translational
- Abstract
Screening of a number of unrelated strains of Escherichia coli confirms the existence of at least two patterns of molecular forms for penicillin-binding protein 1b in E. coli cell envelopes. Our data support that the beta-form of this protein is produced by posttranslational modification of the alpha-form and suggest that the absence of the beta-form in some strains is due to a strain-dependent variability in the alpha-form processing mechanism.
- Published
- 1987
- Full Text
- View/download PDF
566. Carbenicillin resistance of Pseudomonas aeruginosa.
- Author
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Rodríguez-Tebar A, Rojo F, Dámaso D, and Vázquez D
- Subjects
- Carbenicillin metabolism, Carrier Proteins isolation & purification, Carrier Proteins metabolism, Cell Membrane metabolism, Cell Membrane Permeability, Electrophoresis, Polyacrylamide Gel, Humans, In Vitro Techniques, Kinetics, Muramoylpentapeptide Carboxypeptidase isolation & purification, Muramoylpentapeptide Carboxypeptidase metabolism, Penicillin Resistance, Penicillin-Binding Proteins, Pseudomonas aeruginosa isolation & purification, Pseudomonas aeruginosa metabolism, beta-Lactamases metabolism, Bacterial Proteins, Carbenicillin pharmacology, Hexosyltransferases, Peptidyl Transferases, Pseudomonas aeruginosa drug effects
- Abstract
Four strains of Pseudomonas aeruginosa obtained from clinical isolates which are carbenicillin resistant were studied to find the cause(s) of resistance to this beta-lactam antibiotic. The electrophoresis patterns of the four strains (PH20610, PH20815, PH4011, and PH4301) were found to be different from those of a wild-type strain, P. aeruginosa NCTC 10662, and appeared to lack penicillin-binding protein 2. Affinity of other penicillin-binding proteins from strains PH20610 and PH20815 for carbenicillin seemed to be normal or slightly diminished. Electrophoretic patterns of penicillin-binding proteins from strains PH4011 and PH4301 had more profound differences, since the affinities of their penicillin-binding proteins 1a, 1b, and 4 for carbenicillin were decreased by nearly two orders of magnitude relative to the preparations from the wild-type strain. Kinetic studies on binding of carbenicillin to penicillin-binding proteins both in isolated membrane preparations and in intact cells revealed that carbenicillin penetration into resistant cells was a much slower process than in susceptible cells, suggesting that the outer envelope structures serve as an efficient barrier against carbenicillin entry into our P. aeruginosa strains from clinical isolates.
- Published
- 1982
- Full Text
- View/download PDF
567. Interaction of beta-lactam antibiotics with penicillin-binding proteins from Bacillus megaterium.
- Author
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Rodríguez-Tébar A, Rojo F, and Vázquez D
- Subjects
- Anti-Bacterial Agents pharmacology, Bacillus megaterium drug effects, Bacillus megaterium growth & development, Binding, Competitive, Cell Membrane metabolism, Penicillin-Binding Proteins, Protein Binding, beta-Lactams metabolism, beta-Lactams pharmacology, Anti-Bacterial Agents metabolism, Bacillus megaterium metabolism, Bacterial Proteins, Carrier Proteins metabolism, Hexosyltransferases, Muramoylpentapeptide Carboxypeptidase, Peptidyl Transferases
- Abstract
The binding properties of 25 beta-lactam antibiotics to Bacillus megaterium membranes have been studied. The affinities of the antibiotics for the penicillin-binding proteins (PBPs) are also reported. We found that PBP 4 has the highest affinity for nearly all the antibiotics studied whereas PBP 5 has the lowest affinity. Both PBP 4 and PBP 5 appear to be dispensable for the maintenance of bacterial growth and survival and appear to be DD-carboxypeptidases. Only the beta-lactam cefmetazol bound preferentially to PBP 5 and has been used to study the inhibition of DD-carboxypeptidase. Comparative studies with beta-lactam that simultaneously result in (a) binding to PBPs 1 and 3, (b) inhibition of cell growth and (c) lysis, stressed the importance of PBPs 1 and 3 for cell growth and survival.
- Published
- 1982
- Full Text
- View/download PDF
568. Prospects for laboratory engineering of bacteria to degrade pollutants.
- Author
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Timmis KN, Rojo F, and Ramos JL
- Subjects
- Bacteria genetics, Bacteria metabolism, Biodegradation, Environmental, Biological Evolution, Environmental Microbiology, Environmental Pollutants, Genetic Engineering
- Published
- 1988
- Full Text
- View/download PDF
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