Search results for " Reading"

showing 10 items of 463 documents

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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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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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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Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransf…

1990

A detailed analysis of the 8130-bp open reading frame (ORF) of gene toxA and of an upstream ORF designated utxA, indicates the presence of a transcription terminator stem-loop for toxA, promoter sequences, and Shine-Dalgarno boxes for toxA and utxA. No transcription terminator between toxA and utxA is suggested by the sequence. ToxA contains two domains, one-third (C-terminal) with a repetitive structure and the residual two-thirds with no repetitions. The 2499-bp sequence encoding the repetitive structure is composed of nine groups of different short repetitive oligodeoxyribonucleotides (SRONs). A combination of these SRONs codes for five groups of combined repetitive oligopeptides (CROPs)…

DNA BacterialTranscription GeneticSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingBiologyHomology (biology)Conserved sequenceEnterotoxinsOpen Reading FramesSequence Homology Nucleic AcidGeneticsAmino Acid SequencePeptide sequenceGeneRepetitive Sequences Nucleic AcidGeneticsBase SequenceNucleic acid sequenceStreptococcusGeneral MedicineMolecular biologyOpen reading frameTerminator (genetics)Genes BacterialGlucosyltransferasesGene
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Cloning of a cDNA fragment encoding part of the protein moiety of the 58-kDa fibrinogen-binding mannoprotein of Candida albicans

2006

Immunoscreening of a Candida albicans expression library with antibodies against the 58 kDa fibrinogen-binding mannoprotein (mp58) of the fungus resulted in the isolation of clones encoding the protein moiety of this molecule. Sequence of the 0.9 kb cDNA of one of the clones selected for further analysis, revealed an open reading frame coding for 292 amino acids, which displays sequence similarity to proteins belonging to a family of immunodominant antigens of Aspergillus spp. The gene corresponding to this cDNA was named FBP1 (fibrinogen-binding protein). These results represent the first report on the identification of C. albicans genes encoding surface receptors for host proteins.

DNA ComplementaryGenes FungalMolecular Sequence DataSequence alignmentMicrobiologyFungal ProteinsCell WallComplementary DNAImmunoscreeningCandida albicansCell AdhesionGeneticsAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyPeptide sequenceBase SequenceSequence Homology Amino AcidbiologyFibrinogenFibrinogen bindingbiology.organism_classificationMolecular biologyCorpus albicansMolecular WeightBlotting SouthernOpen reading frameCell Adhesion MoleculesSequence AlignmentFEMS Microbiology Letters
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An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.

1996

Abstract We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp 227 -His 428 -Asp 350 in the M. sexta protein) were present, as was the conserved Trp 154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catab…

DNA ComplementaryMolecular Sequence DataBiophysicsSequence HomologyBiologyBiochemistryPolymerase Chain ReactionMiceOpen Reading FramesComplementary DNAMicrosomesCatalytic triadAnimalsHumansAmino Acid SequenceEpoxide hydrolaseMolecular BiologyPeptide sequenceConserved SequenceEpoxide HydrolasesBase SequenceCell BiologyRatsJuvenile HormonesBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesJuvenile hormoneRabbitsOxyanion holeBiochemical and biophysical research communications
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Isolation and characterization of a cDNA encoding a potential morphogen from the marine sponge Geodia cydonium that is conserved in higher metazoans.

1998

Species belonging to the lowest metazoan phylum, the sponges (Porifera), exhibit a surprisingly complex and multifaceted Bauplan (body plan). Recently, key molecules have been isolated from sponges which demonstrate that the cells of these animals are provided with characteristic metazoan adhesion and signal transduction molecules, allowing tissue formation. In order to understand which factors control the spatial organization of these cells in the sponge body plan, we screened for a cDNA encoding a soluble modulator of the behaviour of endothelial cells. A cDNA encoding a putative protein, which is highly similar to the human and mouse endothelial monocyte-activating polypeptide (EMAP) II …

DNA ComplementaryMolecular Sequence DataSequence alignmentGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceMiceComplementary DNAMorphogenesisAnimalsHumansAmino Acid SequencePeptide sequenceCaenorhabditis elegansConserved SequencePhylogenyGeneral Environmental ScienceGeneral Immunology and MicrobiologybiologyProteinsRNA-Binding ProteinsGeneral Medicinebiology.organism_classificationMolecular biologyNeoplasm ProteinsPoriferaSpongeOpen reading frameBiochemistryCosmidCytokinesGeneral Agricultural and Biological SciencesSequence AlignmentResearch ArticleProceedings. Biological sciences
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Cloning and expression of a cDNA copy of the viral K28 killer toxin gene in yeast

1995

The killer toxin K28, secreted by certain killer strains of the yeast Saccharomyces cerevisiae is genetically encoded by a 1.9 kb double-stranded RNA, M-dsRNA (M28), that is present within the cell as a cytoplasmically inherited virus-like particle (VLP). For stable maintenance and replication, M28-VLPs depend on a second dsRNA virus (LA), which has been shown to encode the major capsid protein (cap) and a capsid-polymerase fusion protein (cap-pol) that provides the toxin-coding M-satellites with their transcription and replicase functions. K28 toxin-coding M28-VLPs were isolated, purified and used in vitro for the synthesis of the single-stranded M28 transcript, which was shown to be of pl…

DNA ComplementarySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular Sequence DataGene ExpressionRNA-dependent RNA polymeraseSaccharomyces cerevisiaeBiologyOpen Reading FramesTranscription (biology)Complementary DNAGene expressionGeneticsAmino Acid SequenceCloning MolecularProtein PrecursorsMolecular BiologyGeneRNA Double-StrandedBase SequenceSequence Analysis RNANucleic acid sequenceRNARNA FungalDNA-Directed RNA PolymerasesSequence Analysis DNAMycotoxinsMolecular biologyKiller Factors YeastOpen reading frameProtein BiosynthesisNucleic Acid ConformationRNA ViralMolecular and General Genetics MGG
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Identification and Expression of the SOS Response, aidB-Like, Gene in the Marine Sponge Geodia cydonium: Implication for the Phylogenetic Relationshi…

1998

Sponges (Porifera) are the phylogenetically oldest metazoan organisms. From one member of the siliceous sponges, Geodia cydonium, the cDNA encoding a putative SOS protein, the AidB-like protein of the Ada system from bacteria, was isolated and characterized. The cDNA, GCaidB, comprises an open reading frame of 446 amino acid (aa) residues encoding a polypeptide with a calculated Mr of 49,335. This molecule shows high similarity to the bacterial AidB proteins from Mycobacterium tuberculosis and Escherichia coli and somewhat lower similarities to acyl-CoA dehydrogenases (ADHs) and acyl-CoA oxidases (AOXs). Northern blot analysis confirmed the presence of the complete transcript. The deduced s…

DNA ComplementarySequence analysisMolecular Sequence DataSequence alignmentBiologymedicine.disease_causeAcyl-CoA DehydrogenaseEvolution MolecularBacterial ProteinsPhylogeneticsComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSOS Response GeneticsMolecular BiologyGeneEscherichia coliPeptide sequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsBase SequenceEscherichia coli ProteinsAcyl-CoA Dehydrogenase Long-ChainSequence Analysis DNABlotting NorthernInvertebratesPoriferaOpen reading frameBiochemistryOxidoreductasesSequence AlignmentJournal of Molecular Evolution
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Cloning and expression of new receptors belonging to the immunoglobulin superfamily from the marine sponge Geodia cydonium

1999

A cDNA encoding a receptor tyrosine kinase (RTK) was previously cloned and expressed from the marine sponge (Porifera) Geodia cydonium. In addition to the two intracellular regions characteristic for RTKs, two immunoglobulin (Ig)-like domains are found in the extracellular part of the sponge RTK. In the present study it is shown that no further Ig-like domain is present in the upstream region of the cDNA as well as of the gene hitherto known from the sponge RTK. Two different full-length cDNAs have been isolated and characterized in the present study, which possess two Ig-like domains, one transmembrane segment, and only a short intracellular part, without a TK domain. The two deduced polyp…

DNA ComplementaryTranscription GeneticMolecular Sequence DataImmunologyImmunoglobulinsBiologyReceptor tyrosine kinaseComplementary DNAGeneticsAnimalsHumansAmino Acid SequenceNorthern blotReceptors ImmunologicPeptide Chain Initiation TranslationalIntracellular partPolymorphism GeneticBase SequenceReceptor Protein-Tyrosine KinasesBlotting NorthernImmunohistochemistryMolecular biologyPoriferaProtein Structure TertiaryTransplantationOpen reading frameTransmembrane domainbiology.proteinImmunoglobulin superfamilyCell Adhesion MoleculesImmunogenetics
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