Search results for "Dictyostelium discoideum"

showing 3 items of 3 documents

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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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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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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