Search results for "(Escherichia coli)"

showing 10 items of 689 documents

Citrate Sensing by the C 4 -Dicarboxylate/Citrate Sensor Kinase DcuS of Escherichia coli : Binding Site and Conversion of DcuS to a C 4 -Dicarboxylat…

2007

ABSTRACT The histidine protein kinase DcuS of Escherichia coli senses C 4 -dicarboxylates and citrate by a periplasmic domain. The closely related sensor kinase CitA binds citrate, but no C 4 -dicarboxylates, by a homologous periplasmic domain. CitA is known to bind the three carboxylate and the hydroxyl groups of citrate by sites C1, C2, C3, and H. DcuS requires the same sites for C 4 -dicarboxylate sensing, but only C2 and C3 are highly conserved. It is shown here that sensing of citrate by DcuS required the same sites. Binding of citrate to DcuS, therefore, was similar to binding of C 4 -dicarboxylates but different from that of citrate binding in CitA. DcuS could be converted to a C 4 -…

chemistry.chemical_classificationPeriplasmic spacePlasma protein bindingBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundEnzymechemistryBiochemistrymedicineBinding siteCitric acidMolecular BiologyEscherichia coliPeptide sequenceHistidineJournal of Bacteriology
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Antimicrobial activity of methylene blue and toluidine blue O covalently bound to a modified silicone polymer surface

2009

Methylene Blue or Toluidine Blue O were covalently bound to an activated silicone polymer by means of an amide condensation reaction. UV-visible absorption spectra confirmed that the dye was surface bound. The new polymers with covalently attached dye display significant bactericidal activity against Escherichia coli and Staphylococcus epidermidis with a 99.999% reduction in viable bacteria after four minutes exposure to a low power laser.

chemistry.chemical_classificationRMAbsorption spectroscopybiologyGeneral ChemistryPolymerPhotochemistrybiology.organism_classificationCondensation reactionmedicine.disease_causeRSchemistry.chemical_compoundchemistryCovalent bondStaphylococcus epidermidisAmidePolymer chemistryMaterials ChemistrymedicineEscherichia coliMethylene blueJournal of Materials Chemistry
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The Aerobic and Anaerobic Respiratory Chain of Escherichia coli and Salmonella enterica: Enzymes and Energetics.

2014

Escherichia coli contains a versatile respiratory chain that oxidizes 10 different electron donor substrates and transfers the electrons to terminal reductases or oxidases for the reduction of six different electron acceptors. Salmonella is able to use two more electron acceptors. The variation is further increased by the presence of isoenzymes for some substrates. A large number of respiratory pathways can be established by combining different electron donors and acceptors. The respiratory dehydrogenases use quinones as the electron acceptors that are oxidized by the terminal reductase and oxidases. The enzymes vary largely with respect to their composition, architecture, membrane topolog…

chemistry.chemical_classificationRespiratory chainElectron donorBiologyElectron acceptormedicine.disease_causeMicrobiologyElectron transport chainRedoxIsozymechemistry.chemical_compoundEnzymeBiochemistrychemistrymedicineEscherichia coliEcoSal Plus
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Contact sites of peptide-oligoribonucleotide cross-links identified by a combination of peptide and nucleotide sequencing with MALDI MS.

1997

We have investigated peptide–oligoribonucleotide complexes isolated from cross-linked Escherichia coli 30S ribosomal subunits in order to identify the contact sites of these complexes at the molecular level. For this purpose, reversed-phase (RP) HPLC-purified peptide–oligoribonucleotide complexes were submitted to N-terminal amino acid sequencing in order to determine the cross-linked peptide moiety and were analyzed using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) for calculation of the nucleotide composition of the cross-linked complex. Subsequently, for nucleotide sequence information the complexes were partially hydrolyzed or treated with exonucleases and a…

chemistry.chemical_classificationRibosomal ProteinsBinding SitesBase SequenceChemistryMolecular Sequence DataNucleic acid sequencePeptideRibosomal RNABiochemistryRibosomeAmino acidRNA BacterialBiochemistryBacterial ProteinsRibosomal proteinRNA RibosomalSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationEscherichia coli30SAmino Acid SequencePeptide sequenceJournal of protein chemistry
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Polymer-induced phase separation in suspensions of bacteria

2010

We study phase separation in suspensions of two unrelated species of rod-like bacteria, Escherichia coli and Sinorhizobium meliloti, induced by the addition of two different anionic polyelectrolytes, sodium polystyrene sulfonate or succinoglycan, the former being synthetic and the latter of natural origin. Comparison with the known behaviour of synthetic colloid-polymer mixtures and with simulations show that "depletion" (or, equivalently, "macromolecular crowding") is the dominant mechanism: exclusion of the non-adsorbing polymer from the region between two neighbouring bacteria creates an unbalanced osmotic force pushing them together. The implications of our results for understanding phe…

chemistry.chemical_classificationSinorhizobium melilotiADSORPTIONbiologyBiofilmMIXTURESfood and beveragesGeneral Physics and AstronomyPolymerAGGREGATIONbiology.organism_classificationmedicine.disease_causeLIGHT-SCATTERINGSUCCINOGLYCANPolyelectrolytechemistryESCHERICHIA-COLImedicineBiophysicsMacromolecular crowdingSodium Polystyrene SulfonateEscherichia coliBEHAVIORBacteriaEPL (Europhysics Letters)
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Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme responsible for acp3U formation at position 47 in Escherichia coli tRNAs

2019

AbstracttRNAs from all domains of life contain modified nucleotides. However, even for the experimentally most thoroughly characterized model organism Escherichia coli not all tRNA modification enzymes are known. In particular, no enzyme has been found yet for introducing the acp3U modification at position 47 in the variable loop of eight E. coli tRNAs. Here we identify the so far functionally uncharacterized YfiP protein as the SAM-dependent 3-amino-3-carboxypropyl transferase catalyzing this modification and thereby extend the list of known tRNA modification enzymes in E. coli. Similar to the Tsr3 enzymes that introduce acp modifications at U or m1Ψ nucleotides in rRNAs this protein conta…

chemistry.chemical_classificationTRNA modificationAlkyl and Aryl TransferasesNucleic Acid EnzymesNucleotidesRNASaccharomyces cerevisiaeBiologymedicine.disease_causePhenotypeEnzymechemistryBiochemistryBacterial ProteinsRNA TransferTransfer RNAGeneticsmedicineEscherichia coliTransferaseNucleic Acid ConformationNucleotideEscherichia coliNucleic Acids Research
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The dcuD (former yhcL ) gene product of Escherichia coli as a member of the DcuC family of C4-dicarboxylate carriers: lack of evident expression

1999

The dcuD gene (formerly yhcL) of Escherichia coli shows significant sequence similarity only to the dcuC gene of E. coli, which encodes a C4-dicarboxylate carrier (DcuC) that functions during anaerobic growth. Inactivation of dcuD had no effect on the growth of E. coli under a large number of conditions and led to no detectable changes in phenotype. Translational dcuD'-'lacZ gene fusions were not significantly expressed in the presence of dicarboxylates or monocarboxylates under oxic or anoxic conditions. Other potential substrates such as amino sugar derivatives, amino acids, and alpha-aspartyl dipeptides also did not lead to expression of dcuD. Changes in medium composition, pH, ionic str…

chemistry.chemical_classificationbiologyHypothetical proteinGeneral Medicinebiology.organism_classificationmedicine.disease_causeBiochemistryMicrobiologyEnterobacteriaceaeAmino acidGene productOpen reading frameBiochemistrychemistryGene expressionGeneticsmedicineMolecular BiologyEscherichia coliGeneArchives of Microbiology
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The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of theα/β hydrolase super fa…

2000

The biosynthesis of the anti-arrhythmic alkaloid ajmaline is catalysed by more than 10 specific enzymes. In this multistep process polyneuridine aldehyde esterase (PNAE) catalyses a central reaction by transforming polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmalane skeleton. PNAE was purified from cell suspension cultures of Rauvolfia serpentina. The N-terminal sequence and endoproteinase LysC fragments of the purified protein were used for primer design and for the amplification of specific PCR products leading to the isolation of PNAE-encoding cDNA from a R. serpentina library. The PNAE cDNA was fused with a C-terminal His-tag, …

chemistry.chemical_classificationbiologyStereochemistrymedicine.disease_causebiology.organism_classificationBiochemistryPolyneuridine-aldehyde esterasechemistry.chemical_compoundEnzymeBiosynthesischemistryBiochemistryRauvolfia serpentinaComplementary DNAHydrolasemedicineHeterologous expressionEscherichia coliEuropean Journal of Biochemistry
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Identification of Gip as a novel phage-encoded gyrase inhibitor protein featuring a broad activity profile

2021

AbstractBacteriophages represent a powerful source for the identification of novel antimicrobial proteins. In this study, a screening of small cytoplasmic proteins encoded by the CGP3 prophage of Corynebacterium glutamicum, resulted in the identification of the novel gyrase-inhibiting protein Cg1978 (Gip), which shows a direct interaction with the gyrase subunit A (GyrA). In vitro supercoiling assays further suggest a stabilization of the cleavage complex by Gip. Overproduction of Gip in C. glutamicum resulted in a severe growth defect as well as an induction of the SOS response. The cells adapted to gip overexpression by increasing expression levels of gyrAB and by reducing topA expression…

chemistry.chemical_compoundBiochemistrychemistryProtein subunitmedicineDNA supercoilSOS responsemedicine.disease_causeDNA gyraseEscherichia coliProphageDNACorynebacterium glutamicum
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Genetic Systems for Monitoring Interactions of Transmembrane Domains in Bacterial Membranes

2013

In recent years several systems have been developed to study interactions of TM domains within the inner membrane of the Gram-negative bacterium Escherichia coli. Mostly, a transmembrane domain of interest is fused to a soluble DNA-binding domain, which dimerizes in E. coli cytoplasm after interactions of the transmembrane domains. The dimeric DNA-binding domain subsequently binds to a promoter/operator region and thereby activates or represses a reporter gene. In 1996 the first bacterial system has been introduced to measure interactions of TM helices within a bacterial membrane, which is based on fusion of a transmembrane helix of interest to the DNA-binding domain of the Vibrio cholerae …

chemistry.chemical_compoundTransmembrane domainReporter geneOperator (biology)chemistryCytoplasmmedicineBiophysicsInner membranemedicine.disease_causeEscherichia coliDNADomain (software engineering)
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