Search results for "alignment"

showing 10 items of 627 documents

In vitro and in vivo sulfate reduction in the gut contents of the termite Mastotermes darwiniensis and the rose-chafer Pachnoda marginata.

2005

Sulfate-reducing bacteria (SRB) from termites have been assigned to the genus Desulfovibrio. Desulfovibrio intestinalis lives in the gut of the Australian termite Mastotermes darwiniensis. For the first time we were able to enrich and identify a sulfate-reducing bacterium from the gut of the rose-chafer Pachnoda marginata, which showed the highest 16S rDNA sequence identity (93%) to Desulfovibrio intestinalis and Desulfovibrio strain STL1. Compared to Mastotermes darwiniensis (1x10(7) cells of SRB per ml gut contents), sulfate-reducing bacteria occurred in higher numbers in the gut contents of Pachnoda marginata reaching cell titers of up to 2x10(8) cells per ml gut contents. In vitro sulfa…

DNA BacterialSulfur metabolismIsopteraBiologyApplied Microbiology and BiotechnologyMicrobiologyPachnoda marginataPolymerase Chain ReactionMicrobiologychemistry.chemical_compoundMastotermes darwiniensisRNA Ribosomal 16SAnimalsSulfatePhylogenyBase SequenceSulfatesRibosomal RNAbiology.organism_classification16S ribosomal RNADesulfovibrioColeopterachemistryDesulfovibrioDigestive SystemOxidation-ReductionSequence AlignmentBacteriaThe Journal of general and applied microbiology
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Simultaneous detection of Carnobacterium and Leuconostoc in meat products by multiplex PCR.

2004

M.C. MACIAN, E. CHENOLL AND R. AZNAR. 2004. Aims: To develop a multiplex PCR approach for simultaneous detection of Leuconostoc and Carnobacterium and its validation in meat products. Methods and Results: Two multiplex PCR assays were developed using newly designed 16S rDNA-directed primers adapted to the current taxonomic situation of genera Leuconostoc and Carnobacterium that allow: (i) simultaneous detection of both genera, and members of the nonmotile species of genus Carnobacterium and (ii) identification in a single assay of the nonmotile species C. divergens, C. maltaromicum and C. gallinarum. Sensitivity values of 10 3 and 10 4 CFU g )1 were determined for multiplex PCR detection of…

DNA BacterialTurkeysSwineFood spoilageBiologyCarnobacteriumApplied Microbiology and BiotechnologyPolymerase Chain Reactionlaw.inventionMicrobiologylawMultiplex polymerase chain reactionLeuconostocAnimalsBase sequencePolymerase chain reactionAnalysis methodDNA PrimersBase Sequencefood and beveragesReproducibility of ResultsGeneral Medicinebiology.organism_classificationGenus CarnobacteriumMeat ProductsLactobacillaceaeChickensSequence AlignmentLeuconostocBiotechnologyJournal of applied microbiology
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Arginine kinase in the demosponge Suberites domuncula:regulation of its expression and catalytic activity by silicic acid

2005

SUMMARY In Demospongiae (phylum Porifera) the formation of the siliceous skeleton,composed of spicules, is an energetically expensive reaction. The present study demonstrates that primmorphs from the demosponge Suberites domuncula express the gene for arginine kinase after exposure to exogenous silicic acid. The deduced sponge arginine kinase sequence displays the two characteristic domains of the ATP:guanido phosphotransferases; it can be grouped to the `usual' mono-domain 40 kDa guanidino kinases (arginine kinases). Phylogenetic studies indicate that the metazoan guanidino kinases evolved from this ancestral sponge enzyme; among them are also the `unusual'two-domain 80 kDa guanidino kinas…

DNA ComplementaryArgininePhysiologyMolecular Sequence DataSilicic AcidAquatic ScienceCatalysisGene Expression Regulation EnzymologicEvolution Molecularchemistry.chemical_compoundDemospongeMicroscopy Electron TransmissionAnimalsCluster AnalysisAmino Acid SequenceNorthern blotSilicic acidMolecular BiologyIn Situ HybridizationPhylogenyEcology Evolution Behavior and Systematicschemistry.chemical_classificationBase SequencebiologyKinaseArginine KinaseSequence Analysis DNAArginine kinaseBlotting Northernbiology.organism_classificationPoriferaSuberites domunculaEnzymechemistryBiochemistryInsect Sciencebiology.proteinAnimal Science and ZoologySequence AlignmentJournal of Experimental Biology
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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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Isolation of Mhc class I cDNAs from the axolotl Ambystoma mexicanum.

1997

Class I major histocompatibility complex (Mhc) cDNA clones were isolated from axolotl mRNA by polymerase chain reaction (PCR) and by screening a cDNA phage library. The nucleotide and predicted amino acid sequences show definite similarities to the Mhc class Ialpha molecules of higher vertebrates. Most of the amino acids in the peptide binding region that dock peptides at their N and C termini in mammals are conserved. Several amino acids considered to be important for the interaction of beta2-microglobulin with the Mhc alpha chain are also conserved in the axolotl sequence. The fact that axolotl class I A cDNAs are ubiquitously expressed and highly polymorphic in the alpha1 and alpha2 doma…

DNA ComplementaryImmunologyMolecular Sequence DataGene ExpressionGenes MHC Class IPeptide bindingMajor histocompatibility complexAxolotlComplementary DNASequence Homology Nucleic AcidMHC class IGeneticsAnimalsTissue DistributionAmino Acid SequenceCloning MolecularAmbystoma mexicanumGenechemistry.chemical_classificationGeneticsBinding SitesPolymorphism GeneticbiologyBase SequenceSequence Homology Amino Acidbiology.organism_classificationAmino acidProtein Structure TertiaryAmbystoma mexicanumchemistrybiology.proteinSequence AlignmentImmunogenetics
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Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins

2007

Hexamerins are large storage proteins of insects in the 500 kDa range that evolved from the copper-containing hemocyanins. Hexamerins have been found at high concentration in the hemolymph of many insect taxa, but have remained unstudied in relatively basal taxa. To obtain more detailed insight about early hexamerin evolution, we have studied hexamerins in stoneflies (Plecoptera). Stoneflies are also the only insects for which a functional hemocyanin is known to co-occur with hexamerins in the hemolymph. Here, we identified hexamerins in five plecopteran species and obtained partial cDNA sequences from Perla marginata (Perlidae), Nemoura sp. (Nemouridae), Taeniopteryx burksi (Taeniopterygid…

DNA ComplementaryInsectaMolecular Sequence DataZoologyPerlidaeBiochemistryEvolution MolecularSequence Analysis ProteinPhylogeneticsBotanyHemolymphAnimalsCapniidaeAmino Acid SequenceCloning MolecularMolecular clockMolecular BiologyPhylogenyTaeniopterygidaebiologyPhylogenetic treeSequence Analysis DNANemouridaebiology.organism_classificationInsect ScienceInsect ProteinsSequence AlignmentInsect Biochemistry and Molecular Biology
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Molecular characterization of hemocyanin and hexamerin from the firebrat Thermobia domestica (Zygentoma).

2008

Hexapods possess a tracheal system that enables the transport of oxygen to the inner organs. Although respiratory proteins have been considered unnecessary in most Hexapoda for this reason, we recently showed the presence of a functional hemocyanin in the stonefly Perla marginata. Here we report the identification and molecular characterization of a hemocyanin from Zygentoma (Thysanura). We obtained the full length cDNA of two distinct subunit types from the firebrat Thermobia domestica, and partial sequences of the orthologs from the silverfish Lepisma saccharina. The native T. domestica hemocyanin subunits both consist of 658 amino acids, but a signal peptide for transmembrane transport i…

DNA ComplementaryInsectaProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiochemistrychemistry.chemical_compoundSequence Analysis ProteinHemolymphHemolymphAromatic amino acidsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPhylogenybiologyHemocyaninbiology.organism_classificationThysanuraProtein SubunitschemistryBiochemistryInsect ScienceHemocyaninsInsect ProteinsThermobiaPterygota (plant)FirebratSequence AlignmentInsect biochemistry and molecular biology
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Cloning and sequencing of the cDNA encoding human glutaredoxin.

1994

Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions. We have isolated a cDNA that encodes glutaredoxin from a human brain cDNA library. The encoded protein contains 106 amino acids with a calculated molecular mass of 11.76 kDa and an isoelectric point of 8.09. The amino acid sequence deduced from the cDNA is more than 80% identical to those of other mammalian glutaredoxins.

DNA ComplementaryMolecular Sequence DataBiophysicsSequence alignmentMolecular cloningBiologyBiochemistryStructural BiologyGlutaredoxinComplementary DNAGeneticsHumansAmino Acid SequenceCloning MolecularPeptide sequenceGlutaredoxinschemistry.chemical_classificationBase SequencecDNA libraryNucleic acid sequenceBrainProteinsMolecular biologyAmino acidchemistryBiochemistryOxidoreductasesBiochimica et biophysica acta
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Evolutionary relationships of the metazoan βγ–crystallins, including that from the marine spongeGeodia cydonium

1997

beta gamma-crystallins are one major component of vertebrate lenses. Here the isolation and characterization of a cDNA, coding for the first beta gamma-crystallin molecule from an invertebrate species, the marine sponge Geodia cydonium, is described. The size of the transcript as determined by Northern blotting was 0.7 kb in length. The deduced amino acid sequence consists of 163 aa residues and comprises four repeated motifs which compose the two domains of the beta gamma-crystallin. Motif 3 contains the characteristic beta gamma-crystallin 'Greek key' motif signature, while in each of the three other repeats, one aa residue is replaced by an aa with the same physico-chemical property. The…

DNA ComplementaryMolecular Sequence DataPhysarum polycephalumSequence alignmentPolymerase Chain ReactionGeneral Biochemistry Genetics and Molecular BiologyEvolution MolecularFungal ProteinsPhysarum polycephalumPhylogeneticsComplementary DNAAnimalsHumansAmino Acid SequencePeptide sequencePhylogenyDNA PrimersGene LibraryGeneral Environmental Sciencechemistry.chemical_classificationGeneticsFungal proteinBase SequenceSequence Homology Amino AcidGeneral Immunology and MicrobiologybiologyCoccidioidinGeneral Medicinebiology.organism_classificationCrystallinseye diseasesPoriferaAmino acidSpongechemistryEvolutionary biologysense organsGeneral Agricultural and Biological SciencesSequence AlignmentResearch ArticleProceedings of the Royal Society of London. Series B: Biological Sciences
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Tonoplast subcellular localization of maize cytochrome b5 reductases

2000

Plant cytochrome b 5 reductases (b 5 R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b 5 ) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. Here we report on cDNA cloning of a novel maize b 5 R, NFR II, strongly related to a previously cloned cDNA, NFR I (Bagnaresi et al., 1999, Biochem, J. 338, 499-5051. Maize b 5 R isoforms are produced by a small multi-gene family. The NFR cDNAs were shown to encode active b 5 Rs by heterologous expression in yeast. Both reductases, in addition to Fe 3+ -chelates, efficiently reduced Cu 2+ -chelates. Using a polyclonal antibody able to recogniz…

DNA ComplementaryMolecular Sequence DataSaccharomyces cerevisiaePlant ScienceMolecular cloningBiologyPlant RootsZea maysIsozymeGene Expression Regulation EnzymologicComplementary DNACytochrome b5GeneticsAmino Acid SequenceMicroscopy ImmunoelectronCytochrome ReductasesCytochrome b5 reductaseSequence Homology Amino AcidCytochrome bSequence Analysis DNACell BiologySubcellular localizationMolecular biologyIsoenzymesBiochemistryVacuolesHeterologous expressionSequence AlignmentCytochrome-B(5) ReductaseThe Plant Journal
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