Search results for "GTP Phosphohydrolase"

showing 10 items of 23 documents

A New Method for Extracting Skin Microbes Allows Metagenomic Analysis of Whole-Deep Skin

2013

In the last decade, an extensive effort has been made to characterize the human microbiota, due to its clinical and economic interests. However, a metagenomic approach to the skin microbiota is hampered by the high proportion of host DNA that is recovered. In contrast with the burgeoning field of gut metagenomics, skin metagenomics has been hindered by the absence of an efficient method to avoid sequencing the host DNA. We present here a method for recovering microbial DNA from skin samples, based on a combination of molecular techniques. We have applied this method to mouse skin, and have validated it by standard, quantitative PCR and amplicon sequencing of 16S rRNA. The taxonomic diversit…

Microbial DNAScienceComputational biologyBiologyPolymerase Chain ReactionGTP Phosphohydrolaseslaw.inventionMicelawRNA Ribosomal 16SPell -- MicrobiologiaAnimalsHumansMicrobiomePhylogenyPolymerase chain reactionSkinGeneticsGenètica bacterianaMultidisciplinaryBacteriaintegumentary systemMicrobiotaQRBacterial taxonomyHuman microbiomeDNADNA extractionMice Inbred C57BLMetagenomicsEarth Microbiome ProjectMedicineMetagenomicsResearch ArticleGensPLoS ONE
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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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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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The IFN-γ-Inducible GTPase, Irga6, Protects Mice against Toxoplasma gondii but Not against Plasmodium berghei and Some Other Intracellular Pathogens

2011

Clearance of infection with intracellular pathogens in mice involves interferon-regulated GTPases of the IRG protein family. Experiments with mice genetically deficient in members of this family such as Irgm1(LRG-47), Irgm3(IGTP), and Irgd(IRG-47) has revealed a critical role in microbial clearance, especially for Toxoplasma gondii. The in vivo role of another member of this family, Irga6 (IIGP, IIGP1) has been studied in less detail. We investigated the susceptibility of two independently generated mouse strains deficient in Irga6 to in vivo infection with T. gondii, Mycobacterium tuberculosis, Leishmania mexicana, L. major, Listeria monocytogenes, Anaplasma phagocytophilum and Plasmodium …

Naturwissenschaftliche Fakultät -ohne weitere Spezifikation-Plasmodium bergheiScience-medicine.disease_causeMicrobiologyLeishmania mexicanaGTP PhosphohydrolasesMicrobiologyMiceListeria monocytogenesIn vivoddc:570Parasite Groupsparasitic diseasesmedicineAnimalsLeishmania majorPlasmodium bergheiBiologyMicrobial PathogensPathogenMultidisciplinarybiologyIntracellular parasiteQRImmunityToxoplasma gondiiImmune DefenseMacrophage Activationbiology.organism_classificationVirologyInnate ImmunityBacterial PathogensHost-Pathogen InteractionMice Inbred C57BLMedicineParasitologyToxoplasmaToxoplasmosisResearch ArticlePLoS ONE
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Heterogeneity of KRAS, NRAS, BRAF and PIK3CA mutations in metastatic colorectal cancer and potential effects on therapy in the CAPRI GOIM trial

2015

Background: Evidence suggests that metastatic colorectal carcinoma (mCRC) has a high level of intratumor heterogeneity. We carried out a quantitative assessment of tumor heterogeneity for KRAS, NRAS, BRAF and PIK3CA mutations, in order to assess potential clinical implications. Patients and methods: Tumor samples (n = 182) from the CAPRI-GOIM trial of first-line cetuximab + FOLFIRI in KRAS exon-2 wild-type mCRC patients were assessed by next-generation sequencing that allows quantitative assessment of mutant genes. Mutant allelic frequency was normalized for the neoplastic cell content and, assuming that somatic mutations usually affect one allele, the Heterogeneity Score (HS) was calculate…

OncologyNeuroblastoma RAS viral oncogene homologOrganoplatinum CompoundsColorectal cancerSettore MED/06 - Oncologia MedicaLeucovorinCetuximabCetuximab; Colorectal cancer; Mutations; Next-generation sequencing; Tumor heterogeneity; Antineoplastic Combined Chemotherapy Protocols; Camptothecin; Carcinoma; Cetuximab; Class I Phosphatidylinositol 3-Kinases; Colorectal Neoplasms; Drug Resistance Neoplasm; Fluorouracil; GTP Phosphohydrolases; Gene Frequency; High-Throughput Nucleotide Sequencing; Humans; Leucovorin; Membrane Proteins; Mutation; Organoplatinum Compounds; Phosphatidylinositol 3-Kinases; Proto-Oncogene Proteins B-raf; Proto-Oncogene Proteins p21(ras); Treatment Outcome; Hematology; OncologyColorectal Neoplasmmedicine.disease_causeGTP PhosphohydrolasesGTP PhosphohydrolasePhosphatidylinositol 3-KinasesGene FrequencyAntineoplastic Combined Chemotherapy ProtocolsMembrane ProteinClass I Phosphatidylinositol 3-KinasecolorectalCetuximabHigh-Throughput Nucleotide SequencingHematologyTreatment OutcomeOncologyFOLFIRIKRASFluorouracilColorectal Neoplasmsmedicine.drugHumanProto-Oncogene Proteins B-rafmedicine.medical_specialtyTumor heterogeneityClass I Phosphatidylinositol 3-KinasesProto-Oncogene Proteins p21(ras)Internal medicinemedicinecancerHumansneoplasmsAllele frequencyAntineoplastic Combined Chemotherapy ProtocolSettore MED/08 - ANATOMIA PATOLOGICAbusiness.industryCarcinomaOrganoplatinum CompoundMembrane ProteinsCancermedicine.diseaseColorectal cancerdigestive system diseasesDrug Resistance NeoplasmMutationCancer researchNext-generation sequencingNeoplastic cellCamptothecinPhosphatidylinositol 3-Kinasebusiness
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New findings on primary and acquired resistance to anti-EGFR therapy in metastatic colorectal cancer: Do all roads lead to RAS?

2015

Abstract: Anti-epidermal growth factor receptor therapy with the monoclonal antibodies cetuximab and panitumumab is the main targeted treatment to combine with standard chemotherapy for metastatic colorectal cancer. Many clinical studies have shown the benefit of the addition of these agents for patients without mutations in the EGFR pathway. Many biomarkers, including KRAS and NRAS mutations, BRAF mutations, PIK3CA mutations, PTEN loss, AREG and EREG expression, and HER-2 amplification have already been identified to select responders to anti-EGFR agents. Among these alterations KRAS and NRAS mutations are currently recognized as the best predictive factors for primary resistance. Liquid b…

OncologyNeuroblastoma RAS viral oncogene homologmedicine.medical_specialtyColorectal cancerDrug ResistanceCetuximabAntineoplastic AgentsReviewGene mutationCetuximab; Colorectal cancer; Epidermal growth factor receptor; Panitumumab; RAS; Oncologymedicine.disease_causeAntibodiesGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)Internal medicineMonoclonalmedicinePanitumumabHumansEpidermal growth factor receptorLiquid biopsyNeoplasm MetastasisBiologyneoplasmsbiologyCetuximabEpidermal Growth FactorEpidermal growth factor receptorPanitumumabAntibodies MonoclonalMembrane Proteinsmedicine.diseaseCetuximab; Colorectal cancer; Epidermal growth factor receptor; Panitumumab; RAS; Antibodies Monoclonal; Antineoplastic Agents; Cetuximab; Colorectal Neoplasms; Drug Resistance Neoplasm; GTP Phosphohydrolases; Humans; Membrane Proteins; Mutation; Neoplasm Metastasis; Proto-Oncogene Proteins p21(ras); Receptor Epidermal Growth Factor; OncologyColorectal cancerErbB ReceptorsOncologyDrug Resistance NeoplasmMutationCancer researchbiology.proteinNeoplasmHuman medicineKRASColorectal Neoplasmsmedicine.drugReceptorRAS
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Tyrosine-phosphorylation-dependent and Rho-protein-mediated control of cellular phosphatidylinositol 4,5-bisphosphate levels

1998

The polyphosphoinositide PtdIns(4,5)P2, best known as a substrate for phospholipase C isozymes, has recently been recognized to be involved in a variety of other cellular processes. The aim of this study was to examine whether the cellular levels of this versatile phospholipid are controlled by tyrosine phosphorylation. The studies were performed in human embryonic kidney (HEK)-293 cells stably expressing the M3 muscarinic acetylcholine receptor. Inhibition of tyrosine phosphatases by pervanadate induced an up-to-approx.-2.5-fold increase in the total cellular level of PtdIns(4,5)P2, which was both time- and concentration-dependent. In contrast, the tyrosine kinase inhibitors, genistein and…

Phosphatidylinositol 45-DiphosphateBacterial ToxinsBiologyBiochemistryCell LineGTP Phosphohydrolaseschemistry.chemical_compoundEnzyme activatorBacterial ProteinsGTP-Binding ProteinsPhospholipase DHumansPhosphorylationTyrosinerhoB GTP-Binding ProteinMolecular BiologyPhospholipase CADP-Ribosylation FactorsClostridioides difficilePhospholipase DMembrane ProteinsTyrosine phosphorylationCell BiologyTyrphostinsGenisteinCell biologyEnzyme ActivationBiochemistryPhosphatidylinositol 45-bisphosphatechemistryTyrosinePhosphorylationVanadatesTyrosine kinaseResearch ArticleBiochemical Journal
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Reading the Evolution of Compartmentalization in the Ribosome Assembly Toolbox: The YRG Protein Family.

2016

Reconstructing the transition from a single compartment bacterium to a highly compartmentalized eukaryotic cell is one of the most studied problems of evolutionary cell biology. However, timing and details of the establishment of compartmentalization are unclear and difficult to assess. Here, we propose the use of molecular markers specific to cellular compartments to set up a framework to advance the understanding of this complex intracellular process. Specifically, we use a protein family related to ribosome biogenesis, YRG (YlqF related GTPases), whose evolution is linked to the establishment of cellular compartments, leveraging the current genomic data. We analyzed orthologous proteins …

ProteomesArchaeal ProteinsMycologyBioenergeticsResearch and Analysis MethodsBiochemistryMicrobiologyMolecular EvolutionGTP PhosphohydrolasesEvolution MolecularFungal ProteinsEukaryotic EvolutionBacterial ProteinsFungal EvolutionAnimalsMolecular Biology TechniquesMolecular BiologyEnergy-Producing OrganellesCell NucleusEvolutionary BiologyMolecular Biology Assays and Analysis TechniquesBacterial EvolutionBiology and Life SciencesProteinsPhylogenetic AnalysisBacteriologyNucleolusCell BiologyOrganismal EvolutionCell CompartmentationMitochondriaProtein TransportMicrobial EvolutionCellular Structures and OrganellesRibosomesResearch ArticlePloS one
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A new vicious cycle involving glutamate excitotoxicity, oxidative stress and mitochondrial dynamics

2011

Glutamate excitotoxicity leads to fragmented mitochondria in neurodegenerative diseases, mediated by nitric oxide and S-nitrosylation of dynamin-related protein 1, a mitochondrial outer membrane fission protein. Optic atrophy gene 1 (OPA1) is an inner membrane protein important for mitochondrial fusion. Autosomal dominant optic atrophy (ADOA), caused by mutations in OPA1, is a neurodegenerative disease affecting mainly retinal ganglion cells (RGCs). Here, we showed that OPA1 deficiency in an ADOA model influences N-methyl-D-aspartate (NMDA) receptor expression, which is involved in glutamate excitotoxicity and oxidative stress. Opa1enu/+mice show a slow progressive loss of RGCs, activation …

Retinal Ganglion CellsCancer ResearchReceptor expressionExcitotoxicityApoptosisNeurodegenerativeMitochondrionEyemedicine.disease_causeGTP PhosphohydrolasesMice0302 clinical medicineReceptorsoxidative stressPhosphorylationbcl-2-Associated X Protein0303 health sciencesbiologyGlutamate receptorMitochondriaUp-RegulationCell biologymitochondrial fusionAutosomal DominantOriginal Articlebcl-Associated Death ProteinMitochondrial fissionN-Methyl-D-AspartateBiotechnologymitochondrial fragmentationOncology and CarcinogenesisImmunologybcl-X ProteinSOD2Glutamic AcidReceptors N-Methyl-D-AspartateNMDA receptorsCell Line03 medical and health sciencesCellular and Molecular NeuroscienceBcl-2-associated X proteinOptic Atrophy Autosomal DominantmedicineAnimalsEye Disease and Disorders of Vision030304 developmental biologySuperoxide DismutaseNeurosciencesCell BiologyMolecular biologyeye diseasesOxidative StressOptic AtrophyMutationbiology.proteinOPA1 mutationBiochemistry and Cell Biologysense organsglutamate excitotoxicity030217 neurology & neurosurgeryCell Death & Disease
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Glucosylation of Rho proteins by Clostridium difficile toxin B.

1995

TOXIN A and B, the major virulence factors of Clostridium difficile, are the causative agents of antibiotic-associated pseudomembran-ous colitis. In cultured cell lines their potent cytotoxicity results from their ability to induce disaggregation of the microfilament cytoskeleton1,2. Toxin B acts on the low-molecular-mass GTPase Rho A3,4, which is involved in the regulation of the actin cytoskeleton. We report here that toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid thre-onine at position 37. The modification was identified and localized by tandem electrospray mass spectrometry. UDP-glucose selectively serves as cosubstrate for the monogl…

ThreonineRHOAGlycosylationBacterial ToxinsMolecular Sequence DataClostridium difficile toxin AClostridium difficile toxin Bmacromolecular substancesmedicine.disease_causeMicrofilamentCatalysisMass SpectrometryGTP PhosphohydrolasesBacterial ProteinsGTP-Binding ProteinsmedicineTumor Cells CulturedAnimalsAmino Acid SequenceCytoskeletonActinCells CulturedCytoskeletonMultidisciplinarybiologyToxinClostridioides difficileActin cytoskeletonActinsRecombinant ProteinsRatsGlucoseMarsupialiaBiochemistryGlucosyltransferasesbiology.proteinrhoA GTP-Binding ProteinNature
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