Search results for "amino acid sequence"

showing 10 items of 1296 documents

Cloning and sequencing of the dnaK region of Streptomyces coelicolor A3(2)

1993

Abstract The dnaK homologue of Streptomyces coelicolor A3(2) strain M145 has been cloned and sequenced. Nucleotide sequence analysis of a 2.5-kb region revealed an open reading frame (ORF) encoding a predicted DnaK protein of 618 amino acids (Mr = 66 274). The dnaK coding sequence displays extreme codon bias and shows a strong preference for CGY and GGY, for Arg and Gly codons, respectively. The predicted DnaK sequence has a high Lys:Arg ratio which is not typical of streptomycete proteins. The region immediately downstream from dnaK contains an ORF for a GrpE-like protein; the predicted start codon of grpE overlaps the last two codons of dnaK, indicating that the two genes are translationa…

DNA BacterialMolecular Sequence Datagenetic processesBacterial ProteinsStart codonGeneticsCoding regionHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularCodonGeneHeat-Shock Proteinschemistry.chemical_classificationGeneticsBase SequencebiologyEscherichia coli ProteinsStreptomyces coelicolorNucleic acid sequenceStreptococcusGeneral Medicinebiology.organism_classificationAmino acidOpen reading framechemistryGenes BacterialProtein BiosynthesisCodon usage biasbiological sciencesbacteriaSequence AlignmentGene
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Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in u…

1996

In Escherichia coli, two carriers (DcuA and DcuB) for the transport of C4 dicarboxylates in anaerobic growth were known. Here a novel gene dcuC was identified encoding a secondary carrier (DcuC) for C4 dicarboxylates which is functional in anaerobic growth. The dcuC gene is located at min 14.1 of the E. coli map in the counterclockwise orientation. The dcuC gene combines two open reading frames found in other strains of E. coli K-12. The gene product (DcuC) is responsible for the transport of C4 dicarboxylates in DcuA-DcuB-deficient cells. The triple mutant (dcuA dcuB dcuC) is completely devoid of C4-dicarboxylate transport (exchange and uptake) during anaerobic growth, and the bacteria are…

DNA BacterialMutantMolecular Sequence DataBiologymedicine.disease_causeMicrobiologyGene productBacterial ProteinsmedicineEscherichia coliDicarboxylic AcidsAmino Acid SequenceAnaerobiosisMolecular BiologyEscherichia coliPeptide sequenceGeneDicarboxylic Acid TransportersBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsChromosome MappingBiological Transportbiology.organism_classificationIsoenzymesOpen reading frameMutagenesis InsertionalBiochemistryC4-dicarboxylate transportCarrier ProteinsBacteriaResearch ArticleJournal of bacteriology
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Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibitio…

2000

ABSTRACT Buchnera aphidicola , the prokaryotic endosymbiont of aphids, complements dietary deficiencies with the synthesis and provision of several essential amino acids. We have cloned and sequenced a region of the genome of B. aphidicola isolated from Acyrthosiphon pisum which includes the two-domain aroQ/pheA gene. This gene encodes the bifunctional chorismate mutase-prephenate dehydratase protein, which plays a central role in l -phenylalanine biosynthesis. Two changes involved in the overproduction of this amino acid have been detected. First, the absence of an attenuator region suggests a constitutive expression of this gene. Second, the regulatory domain of the Buchnera prephenate de…

DNA BacterialPhenylalanineMolecular Sequence DataPrephenate dehydratasePhenylalanineMicrobiologychemistry.chemical_compoundBiosynthesisBuchneraEscherichia coliAnimalsHumansAmino Acid SequenceEnzyme InhibitorsSymbiosisMolecular BiologyGenechemistry.chemical_classificationGeneticsBinding SitesbiologyBase SequenceSequence Homology Amino Acidbiochemical phenomena metabolism and nutritionbiology.organism_classificationPrephenate DehydrataseAmino acidEnzymeBiochemistrychemistryDehydrataseAphidsBuchneraGenome BacterialPopulation Genetics and EvolutionChorismate MutaseJournal of bacteriology
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Comparative genomics and proteomics of Helicobacter mustelae, an ulcerogenic and carcinogenic gastric pathogen

2010

Abstract Background Helicobacter mustelae causes gastritis, ulcers and gastric cancer in ferrets and other mustelids. H. mustelae remains the only helicobacter other than H. pylori that causes gastric ulceration and cancer in its natural host. To improve understanding of H. mustelae pathogenesis, and the ulcerogenic and carcinogenic potential of helicobacters in general, we sequenced the H. mustelae genome, and identified 425 expressed proteins in the envelope and cytosolic proteome. Results The H. mustelae genome lacks orthologs of major H. pylori virulence factors including CagA, VacA, BabA, SabA and OipA. However, it encodes ten autotransporter surface proteins, seven of which were detec…

DNA BacterialProteomicslcsh:QH426-470Proteomelcsh:BiotechnologyMolecular Sequence DataVirulenceCarcinogenicHelicobacter mustelaeProteomicsFN555004MicrobiologyUlcerogenic03 medical and health sciencesBacterial ProteinsHelicobacterlcsh:TP248.13-248.65medicineGeneticsCagAHelicobacterAmino Acid SequencePhylogeny030304 developmental biology0303 health sciencesComparative Genomic HybridizationbiologyHelicobacter pyloriVirulence030306 microbiologyCancerGene Expression Regulation BacterialGenomicsSequence Analysis DNAHelicobacter pylorimedicine.diseasebiology.organism_classificationdigestive system diseases3. Good healthlcsh:GeneticsProteomeGastritismedicine.symptomSequence AlignmentH. pyloriGenome BacterialBiotechnologyResearch ArticleBMC Genomics
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Comparative sequence analysis of the Clostridium difficile toxins A and B.

1992

The six clones pTB112, pTB324, pTBs12, pCd122, pCd14 and pCd13 cover the tox locus of Clostridium difficile VPI 10463. This region of 19 kb of chromosomal DNA contains four open reading frames including the complete toxB and toxA genes. The two toxins show 63% amino acid (aa) homology, a relatedness that had been predicted by the cross-reactivity of some monoclonal antibodies (mAb) but that is in contrast to the toxin specificity of polyclonal antisera. A special feature of ToxA and ToxB is their repetitive C-termini. We define herein 19 individual CROPs (combined repetitive oligopeptides of 20-50 aa length) in the ToxB C-terminus, which are separable into five homologous groups. Comparison…

DNA BacterialSequence analysisBacterial ToxinsBlotting WesternMolecular Sequence DataRestriction MappingDNA RecombinantLocus (genetics)Cross ReactionsHomology (biology)EnterotoxinsBacterial ProteinsSequence Homology Nucleic AcidGene duplicationGeneticsAmino Acid SequenceMolecular BiologyGeneRepetitive Sequences Nucleic AcidGeneticsbiologyBase SequenceClostridioides difficileNucleic acid sequenceAntibodies MonoclonalNucleic Acid HybridizationMolecular biologyRecombinant ProteinsOpen reading framePolyclonal antibodiesbiology.proteinMoleculargeneral genetics : MGG
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Definition of the single integration site of the pathogenicity locus in Clostridium difficile.

1996

We determined the nucleotide sequence 3.8 kb upstream and 5.2 kb downstream of the toxin genes A and B of Clostridium difficile. Nine ORFs were discovered. Based on PCR-directed approaches, two were attributed to the pathogenicity locus (PaLoc). The other seven were found in every C. difficile isolate obtained from the human gastrointestinal tract, respectless of their toxinogenicity. The ORFs cdu1 and cdu2/2' upstream of the PaLoc displayed similarity to repressors of Gram-positive bacteria (cdu1), and to an Na+/H+ antiporter described for Enterococcus hirae (cdu2/2'). Downstream of the locus a putative ABC transporter (cdd2-4) was identified. With a set of three paired primers used in pol…

DNA BacterialSequence analysisBacterial ToxinsMolecular Sequence DataVirulenceLocus (genetics)BiologyEnterotoxinsOpen Reading FramesBacterial ProteinsSpecies SpecificityGeneticsHumansAmino Acid SequenceORFSGeneGeneticsBase SequenceSequence Homology Amino AcidVirulenceClostridioides difficileNucleic acid sequenceGeneral MedicineMolecular biologyIntestinesTerminator (genetics)DNA Transposable ElementsATP-Binding Cassette TransportersMobile genetic elementsGene
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Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins.

1993

The T-cell-stimulating activity of staphylococcal enterotoxin B (SEB) is an important factor in the pathogenesis of certain staphylococcal diseases. To investigate the immunologically active domains of the SEB molecule, we have produced truncated fragments of recombinant SEB by C-terminal and N-terminal deletions. The fragments were expressed as fusion proteins with protein A, including a cleavage site to remove the protein A part. Mutant proteins were tested for the ability to stimulate human resting T cells and SEB-reactive T-cell clones. Deletion of only 9 amino acids from the C terminus leads to complete loss of T-cell-stimulating activity. Removing further amino acids from the SEB mole…

DNA BacterialStaphylococcus aureusRecombinant Fusion ProteinsImmunologyMutantMolecular Sequence DataBiologyMicrobiologyEpitopeEnterotoxinsMiceStructure-Activity RelationshipMutant proteinAnimalsAmino Acid SequencePeptide sequencechemistry.chemical_classificationAntigens BacterialMice Inbred BALB CBase SequenceC-terminusFusion proteinMolecular biologyAmino acidInfectious DiseaseschemistryMutationParasitologyGene DeletionConformational epitopeResearch Article
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Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties.

1998

A gene encoding a novel cell wall-associated protein of Staphylococcus saprophyticus that binds fibronectin and to sheep erythrocytes has been cloned and sequenced. The 4392 bp open reading frame codes for an amino acid sequence that is quite similar to the Atl, an autolysin, of Staphylococcus aureus and to the AtlE of S. epidermidis. The two regions of most pronounced homology code for an N-acetyl-muramyl-L-alanine amidase and for an endo-beta-N-acetyl-D-glucosaminidase. The cloned protein lysed cells of S. saprophyticus and Micrococcus luteus exogenously. Subcloning localized the enzymatic activities to the regions of high homology and demonstrated that the interposed sequence is responsi…

DNA BacterialStaphylococcusMolecular Sequence DataBiologyMicrobiologyHomology (biology)BacteriolysisAmino Acid SequenceCloning MolecularAdhesins BacterialMolecular BiologyGenePeptide sequenceAllelesStaphylococcus saprophyticusBinding SitesBase SequenceAutolysinSequence Analysis DNAbiology.organism_classificationMolecular biologyFibronectinsBacterial adhesinOpen reading frameSubcloningHemagglutininsBiochemistryGenes BacterialMolecular microbiology
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Transcription analysis of the genes tcdA-E of the pathogenicity locus of Clostridium difficile.

1997

To analyse the transcription pattern of the five tcdA-E genes of the pathogenicity locus (PaLoc) of Clostridium difficile a protocol was established to purify RNA from strain VPI10463. Transcription analysis of the five tcdA-E genes showed that they were all transcribed. In the early exponential phase, a high level of tcdC and low levels of tcdA,B,D,E transcripts were detectable; this was inverted in the stationary phase, suggesting that TcdC might have a negative influence on transcription of the other genes. Three transcription initiation sites, one for tcdA and two for tcdB were determined by primer extension analysis. Readthrough transcripts from outside the locus were not obtainable, s…

DNA BacterialTranscription GeneticBacterial ToxinsMolecular Sequence DataLocus (genetics)Helix-turn-helixBiologymedicine.disease_causeBiochemistryPolymerase Chain ReactionPrimer extensionchemistry.chemical_compoundEnterotoxinsBacterial ProteinsTranscription (biology)medicineAmino Acid SequencePromoter Regions GeneticGeneDNA PrimersRegulation of gene expressionGeneticsBase SequenceSequence Homology Amino AcidVirulenceClostridioides difficileClostridium perfringensMolecular biologyDNA-Binding ProteinsRepressor ProteinschemistryGenes BacterialDNAEuropean journal of biochemistry
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Inducible metabolism of phenolic acids in Pediococcus pentosaceus is encoded by an autoregulated operon which involves a new class of negative transc…

2000

ABSTRACTPediococcus pentosaceusdisplays a substrate-inducible phenolic acid decarboxylase (PAD) activity onp-coumaric acid. Based on DNA sequence homologies between the three PADs previously cloned, a DNA probe of theLactobacillus plantarum pdcgene was used to screen aP. pentosaceusgenomic library in order to clone the corresponding gene of this bacteria. One clone detected with this probe displayed a low PAD activity. Subcloning of this plasmid insertion allowed us to determine the part of the insert which contains a 534-bp open reading frame (ORF) coding for a 178-amino-acid protein presenting 81.5% of identity withL. plantarumPDC enzyme. This ORF was identified as thepadAgene. A second O…

DNA BacterialTranscription GeneticOperonCarboxy-LyasesMolecular Sequence DataGenetics and Molecular BiologyBiologyMicrobiologyGene Expression Regulation EnzymologicPlasmidBacterial ProteinsSequence Homology Nucleic AcidOperonEscherichia coliHydroxybenzoatesGenomic libraryAmino Acid SequencePediococcusCloning MolecularMolecular BiologyGeneRegulator geneGeneticsBase SequenceSequence Homology Amino Acidfood and beveragesPromoterGene Expression Regulation BacterialSequence Analysis DNAMolecular biologyCulture MediaRepressor ProteinsOpen reading frameLactobacillusSubcloningGenes BacterialJournal of bacteriology
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