Search results for "Dictyostelium"

showing 7 items of 7 documents

RIBOSOMAL SUBUNIT EXCHANGE IN DICTYOSTELIUM PURPUREUM

1970

Carbon IsotopesCell divisionbiologyProtein subunitCell BiologyRibosomal RNATritiumbiology.organism_classificationBrief NotesRibosomeArticleDictyostelium purpureumBotanyMyxomycetesRibosomesCell DivisionJournal of Cell Biology
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Coincidental loss of bacterial virulence in multi-enemy microbial communities.

2014

The coincidental virulence evolution hypothesis suggests that outside-host selection, such as predation, parasitism and resource competition can indirectly affect the virulence of environmentally-growing bacterial pathogens. While there are some examples of coincidental environmental selection for virulence, it is also possible that the resource acquisition and enemy defence is selecting against it. To test these ideas we conducted an evolutionary experiment by exposing the opportunistic pathogen bacterium Serratia marcescens to the particle-feeding ciliate Tetrahymena thermophila, the surfacefeeding amoeba Acanthamoeba castellanii, and the lytic bacteriophage Semad11, in all possible combi…

Ecological selectionBacteriophageNatural SelectionBacteriophagesANTAGONISTIC COEVOLUTIONLISTERIA-MONOCYTOGENESSerratia marcescens1183 Plant biology microbiology virologyGeneticsSERRATIA-MARCESCENSAcanthamoeba castellanii0303 health sciencesMultidisciplinaryEcologybiologyQTetrahymenaRAcanthamoeba castellaniiMedicineResearch ArticleEvolutionary ProcessesVirulence FactorsAntagonistic CoevolutionScienceMicrobial ConsortiaeducationVirulenceMicrobiologyMicrobial EcologyMicrobiologyEvolution Molecular03 medical and health sciencesmulti-enemy microbial communitiesWater environment030304 developmental biologySTAPHYLOCOCCUS-AUREUSEvolutionary BiologyPSEUDOMONAS-AERUGINOSA VIRULENCE030306 microbiologybacterial virulenceDICTYOSTELIUM-DISCOIDEUMBiology and Life SciencesBacteriologybiology.organism_classificationOrganismal EvolutionArtificial SelectionTETRAHYMENA-THERMOPHILAEvolutionary EcologyMicrobial Evolutionta1181AMEBA ACANTHAMOEBA-CASTELLANIILEGIONELLA-PNEUMOPHILABacteriaMEDIA COMPOSITION INFLUENCESPLoS ONE
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Regulated expression and phosphorylation of the 23-26-kDa ras protein in the sponge Geodia cydonium.

1990

We have cloned, sequenced and examined the sponge Geodia cydonium cDNA encoding a protein homologous to ras proteins. The sponge ras protein has a more conserved N-terminal region and a less conserved C-terminal region, especially in comparison to Dictyostelium discoideum; the similarity to human c-Ha-ras-1 and to Saccharomyces cerevisiae is less pronounced. The sponge ras cDNA comprises five TAG triplets; at the translational level these UAG termination codons are suppressed by a Gln-tRNA. The sponge ras protein was isolated and partially purified (23-26 kDa) and found to undergo phosphorylation at a threonine moiety, when dissociated cells were incubated in the presence of a homologous ag…

GTP'Saccharomyces cerevisiaeMolecular Sequence DataGTPaseBiochemistryDictyostelium discoideumProto-Oncogene Proteins p21(ras)Complementary DNASequence Homology Nucleic AcidAnimalsInsulinNCK1Amino Acid SequenceThreonineCloning MolecularPhosphorylationGene LibrarybiologyBase SequenceDNAbiology.organism_classificationMolecular biologyPoriferaMolecular WeightKineticsBiochemistryGene Expression RegulationPhosphorylationEuropean journal of biochemistry
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The Parkinson Disease Gene LRRK2: Evolutionary and Structural Insights

2006

Mutations in the human leucine-rich repeat kinase 2 (LRRK2) gene are associated with both familial and sporadic Parkinson disease (PD). LRRK2 belongs to a gene family known as Roco. Roco genes encode for large proteins with several protein domains. Particularly, all Roco proteins have a characteristic GTPase domain, named Roc, plus a domain of unknown function called COR. In addition, LRRK2 and several other Roco proteins also contain a protein kinase domain. In this study, I use a combination of phylogenetic and structural analyses of the COR, Roc, and kinase domains present in Roco proteins to describe the origin and evolutionary history of LRRK2. Phylogenetic analyses using these domains…

Models MolecularProtein ConformationMolecular Sequence DataProtein domainGTPaseProtein Serine-Threonine KinasesBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-2MAP3K7SH3 domainGTP PhosphohydrolasesEvolution MolecularGeneticsAnimalsHumansDictyosteliumAmino Acid Sequencec-RafMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsGeneticsSequence Homology Amino AcidParkinson DiseaseLRRK2Protein Structure Tertiarynervous system diseasesDisease Models AnimalProtein kinase domainRabProtein KinasesMolecular Biology and Evolution
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Mechanism of Oligomerisation of Cyclase-associated Protein from Dictyostelium discoideum in Solution

2006

Abstract Cyclase-associated protein (CAP) is a highly conserved modular protein implicated in the regulation of actin filament dynamics and a variety of developmental and morphological processes. The protein exists as a high molecular weight complex in cell extracts and purified protein possesses a high tendency to aggregate, a major obstacle for crystallisation. Using a mutagenesis approach, we show that two structural features underlie the mechanism of oligomerisation in Dictyostelium discoideum CAP. Positively charged clusters on the surface of the N-terminal helix-barrel domain are involved in inter-molecular interactions with the N or C-terminal domains. Abolishing these interactions m…

Models MolecularProtein DenaturationProtein FoldingProtein ConformationMolecular Sequence DataOligomerDictyostelium discoideumMass SpectrometryProtein Structure SecondaryProtein–protein interactionProtein filamentchemistry.chemical_compoundProtein structureStructural BiologyEnzyme StabilityAnimalsUreaDictyosteliumAmino Acid SequenceMolecular BiologyActinN capCrystallographybiologyCircular Dichroismbiology.organism_classificationDictyosteliumActinsProtein Structure TertiaryMolecular WeightSolutionsCytoskeletal ProteinschemistryBiochemistryModels ChemicalMutationBiophysicsChromatography GelDimerizationProtein Binding
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Dynamic modulation of Dnmt2-dependent tRNA methylation by the micronutrient queuine

2015

Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs. We report here that the activities of two Dnmt2 homologs, Pmt1 from Schizosaccharomyces pombe and DnmA from Dictyostelium discoideum, are strongly stimulated by prior queuosine (Q) modification of the substrate tRNA. In vivo tRNA methylation levels were stimulated by growth of cells in queuine-containing medium; in vitro Pmt1 activity was enhanced on Q-containing RNA; and queuine-stimulated in vivo methylation was abrogated by the absence of the enzyme that inserts queuine into tRNA, eukaryotic tRNA-guanine transglycosylase. Global analysis of tRNA methylation in S. pombe showed a striking selectivity of Pm…

RNA Transfer AspTRNA modificationGuanineMethyltransferaseTRNA methylationbiologyQueuosineQueuineMethylationbiology.organism_classificationMethylationchemistry.chemical_compoundRNA TransferchemistryBiochemistrySchizosaccharomycesTransfer RNAGeneticsRNADictyosteliumDNA (Cytosine-5-)-MethyltransferasesMicronutrientsPentosyltransferasesSchizosaccharomyces pombe ProteinsSchizosaccharomycesNucleic Acids Research
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The Dnmt2 RNA methyltransferase homolog of Geobacter sulfurreducens specifically methylates tRNA-Glu

2014

Dnmt2 enzymes are conserved in eukaryotes, where they methylate C38 of tRNA-Asp with high activity. Here, the activity of one of the very few prokaryotic Dnmt2 homologs from Geobacter species (GsDnmt2) was investigated. GsDnmt2 was observed to methylate tRNA-Asp from flies and mice. Unexpectedly, it had only a weak activity toward its matching Geobacter tRNA-Asp, but methylated Geobacter tRNA-Glu with good activity. In agreement with this result, we show that tRNA-Glu is methylated in Geobacter while the methylation is absent in tRNA-Asp. The activities of Dnmt2 enzymes from Homo sapiens, Drosophila melanogaster, Schizosaccharomyces pombe and Dictyostelium discoideum for methylation of the …

RNA Transfer AsptRNA MethyltransferasesMethyltransferasebiologyNucleic Acid EnzymesRNAMethylationbiology.organism_classificationMethylationDictyostelium discoideumRNA Transfer GluSubstrate SpecificityMiceBiochemistryBacterial ProteinsTransfer RNASchizosaccharomyces pombeGeneticsAnimalsHumansNucleic Acid ConformationGeobacterGeobacter sulfurreducensGeobacterNucleic Acids Research
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