Search results for "mitochondrial Proteins"

showing 10 items of 87 documents

Tumor suppression inDrosophila is causally related to the function of thelethal(2)tumorous imaginal discs gene, adnaJ homolog

1995

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) causes in homozygotes malignant growth of cells of the imaginal discs and the death of the mutant larvae at the time of puparium formation. We describe the molecular cloning of the l(2)tid+ gene and its temporal expression pattern in the wild-type and mutant alleles. Germ line rescue of the tumor phenotype was achieved with a 7.0 kb Hindlll-fragment derived from the polytene chromosome band 59F5. The l(2)tid+ gene spans approximately 2.5 kb of genomic DNA. The protein coding region, 1,696 bps long, is divided by an intron into two exons. The predicted Tid56 protein contains 518 amino acids and posse…

DNA ComplementarySaccharomyces cerevisiae ProteinsTumor suppressor geneMolecular Sequence DataMutantGenes InsectSaccharomyces cerevisiaeAnimals Genetically ModifiedFungal ProteinsMitochondrial ProteinsSpecies SpecificityEscherichia coliGeneticsAnimalsDrosophila ProteinsHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularGeneAllelesHeat-Shock ProteinsPolytene chromosome bandBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsPupaChromosome MappingExonsNeoplasms ExperimentalCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyImaginal discDrosophila melanogasterLarvaDNAJA2Drosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyDevelopmental Genetics
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Mitochondrial localization and temporal expression of the Drosophila melanogaster DnaJ homologous tumor suppressor Tid50

1998

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (tid) was identified as a homolog of all dnaJ-like genes known to date which have been well preserved in evolution. Homozygous D. melanogaster l(2)tid mutants l(2)tid1, l(2)tid2 and l(2)tid3 are characterized by neoplastic transformation of the adult integumental primordia, the imaginal discs, and the death at the time of puparium formation. The first part of this study is concerned with the identification and subcellular localization of the l(2)tid-encoded protein, Tid50. The second part examines its tissue specific expression during wild-type development and in tumorous imaginal discs. To specify the functi…

Embryo NonmammalianTumor suppressor geneMutantGenes InsectCell FractionationBiochemistryCell LineMitochondrial ProteinsMelanogasterAnimalsDrosophila ProteinsGenes Tumor SuppressorNeoplastic transformationRNA MessengerGeneHeat-Shock ProteinsbiologyPupaGene Expression Regulation DevelopmentalRNANeoplasms ExperimentalSequence Analysis DNAOriginal ArticlesCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyMitochondriaGene Expression Regulation NeoplasticImaginal discDrosophila melanogasterOrgan SpecificityLarvaRabbitsDrosophila melanogasterCell Stress & Chaperones
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Characterization of a novel open reading frame, urf a, in the mitochondrial genome of fission yeast: correlation of urf a mutations with a mitochondr…

1991

Between the genes for tRNA(gin) and tRNA(ile) an open reading frame of 227 amino acids has been identified which is unique among known mitochondrial genomes and which has been termed urf a (Lang et al. 1983; Kornrumpf et al. 1984). It uses the "mitochondrial" genetic code, i.e., it contains a TGA codon, whereas all other protein-encoding genes, and all but one intronic open reading frame, use the "standard" genetic code (UGG for tryptophan). A previous paper has demonstrated that "mutator" strains show an increased formation of mitochondrial drug-resistant and respiration-deficient mutants (including deletions). In this paper we show that the mutator activity is correlated with mutations in…

GlycerolMitochondrial DNAMutantMolecular Sequence DataExtrachromosomal InheritanceBiologymedicine.disease_causeDNA MitochondrialFrameshift mutationFungal ProteinsMitochondrial ProteinsOpen Reading FramesGene Expression Regulation FungalSchizosaccharomycesGeneticsmedicineAmino Acid SequenceCodonDNA FungalFrameshift MutationGeneGeneticsMutationTranslational frameshiftBase SequenceGeneral MedicineGenetic codeOpen reading framePhenotypeMutationSchizosaccharomyces pombe ProteinsCurrent genetics
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Identification of a novel compound heterozygote SCO2 mutation in cytochrome c oxidase deficient fatal infantile cardioencephalomyopathy

2006

UNLABELLED Fatal infantile cardioencephalomyopathy (OMIM No. 604377) is a disorder of the mitochondrial respiratory chain and is characterised by neonatal progressive muscular hypotonia and cardiomyopathy because of severe Cytochrome c oxidase deficiency. Here we report a novel mutation in the Cytochrome c oxidase assembly gene SCO2 in an infant with fatal infantile cardioencephalomyopathy despite normal initial metabolic screening. CONCLUSION In newborns with unexplained muscular hypotonia and cardiomyopathy genetic testing of mitochondrial respiratory chain disorders might be helpful to establish a final diagnosis and guide treatment decisions.

Heterozygotemedicine.medical_specialtyPathologyCardiomyopathyCytochrome-c Oxidase DeficiencyCompound heterozygositymedicine.disease_causeMitochondrial ProteinsFatal OutcomeMitochondrial EncephalomyopathiesInternal medicinemedicineHumansCytochrome c oxidaseGeneGenetic testingMutationMuscular hypotoniamedicine.diagnostic_testbiologybusiness.industryInfantGeneral Medicinemedicine.diseaseEndocrinologyMitochondrial respiratory chainMutationPediatrics Perinatology and Child Healthbiology.proteinFemaleCardiomyopathiesCarrier ProteinsbusinessMolecular ChaperonesActa Paediatrica
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Peroxisome proliferator-activated receptors as regulators of lipid metabolism; tissue differential expression in adipose tissues during cold acclimat…

2004

Brown (BAT) and white (WAT) adipose tissues play a key role in the body energy balance orchestrated by the central nervous system. Hibernators have developed a seasonal obesity to respond to inhospitable environment. Jerboa is one of the deep hibernator originated from sub-desert highlands. Thus, this animal represents an excellent model to study cold adaptation mechanism. We report that the adipogenic factor PPARgamma exhibits a differential expression between BAT and WAT at mRNA level. A specific induction was only seen in WAT of pre-hibernating jerboa. Interestingly, PPAR beta/delta is specifically induced in BAT and brain of pre-hibernating jerboa, highlighting for the first time the po…

Hibernationmedicine.medical_specialtyAcclimatizationPeroxisome Proliferator-Activated ReceptorsPeroxisome proliferator-activated receptorAdipose tissueRodentiaWhite adipose tissueBiologyBiochemistryAcyl-CoA DehydrogenaseIon ChannelsMitochondrial ProteinsClofibric AcidInternal medicineHibernationBrown adipose tissuemedicineAcyl-CoA oxidaseAnimalsRNA MessengerUncoupling Protein 1chemistry.chemical_classificationFibric AcidsMembrane ProteinsGeneral MedicineLipid MetabolismLipidsMitochondriaCold TemperatureEndocrinologymedicine.anatomical_structurechemistryAdipose TissueGene Expression RegulationPhospholipasesCiprofibrateAcyl-CoA OxidaseCarrier ProteinsEnergy MetabolismOxidoreductasesThermogenesismedicine.drugBiochimie
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Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide

2011

DAPIT (Diabetes Associated Protein in Insulin-sensitive Tissues) is a small, phylogenetically conserved, 58 amino acid peptide that was previously shown to be down-regulated at mRNA level in insulin-sensitive tissues of type 1 diabetes rats. In this study we characterize a custom made antibody against DAPIT and confirm the mitochondrial presence of DAPIT on cellular level. We also show that DAPIT is localized in lysosomes of HUVEC and HEK 293T cells. In addition, we describe the histological expression of DAPIT in several tissues of rat and man and show that it is highly expressed especially in cells with high aerobic metabolism and epithelial cells related to active transport of nutrients …

HistologyCellular respirationProtein subunitBiophysicsPeptideV-ATPaseBiologyMitochondrionAntibodiesMitochondrial ProteinsHuman Umbilical Vein Endothelial CellsV-ATPaseAnimalsHumansmitochondrionta315lcsh:QH301-705.5PhylogenyDAPIT mitochondrion V-ATPase type 1 diabeteschemistry.chemical_classificationRegulation of gene expressionOriginal Papertype 1 diabetes.HEK 293 cellsMembrane ProteinsCell BiologyProton PumpsCell biologyMitochondriaRatsHEK293 CellsMembrane proteinchemistryBiochemistryGene Expression Regulationlcsh:Biology (General)Organ SpecificityLysosomesDAPITEuropean Journal of Histochemistry
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Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells

1996

AbstractThe endothelial protein p33/gC1qR is thought to mediate the assembly of components of the kinin-forming and complement-activating pathways on the surface of cardiovascular cells. FACS analysis of intact human umbilical vein endothelial cells using specific antibodies to p33 revealed a minor fluorescence on the cell surface whereas permeabilized cells showed a bright fluorescence indicative of an intracellular localization of p33. Immunostaining of fixed cells confirmed the predominant intracellular localization of p33. Fractionation studies demonstrated that the vesicular but not the membrane fraction of EA.hy926 cells is rich in p33. We conclude that externalization of p33 must pre…

Kininogen bindingp33Kininogen binding proteinCellBiophysicsComplementFluorescent Antibody TechniqueBiologyBiochemistryUmbilical veinMitochondrial ProteinsStructural BiologyGeneticsmedicineHumansMolecular BiologyCells CulturedMembrane GlycoproteinsImmune SeraCell BiologyKininFlow CytometryKininFluorescenceReceptors ComplementCell biologyEndothelial stem cellSpecific antibodyHyaluronan Receptorsmedicine.anatomical_structuregC1qREndothelium VascularCarrier ProteinsImmunostainingFEBS Letters
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Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrati…

2014

It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naive, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naive cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60…

LightCancer Treatmentlcsh:MedicinePlasma protein bindingMitochondrionBiochemistrySmall-Angle ScatteringCell-free systemScatteringchemistry.chemical_compoundCytosolProtein structureBasic Cancer ResearchMacromolecular Structure AnalysisMedicine and Health SciencesScattering RadiationHsp60 Gro EL Recombinant proteinslcsh:ScienceAdenosine TriphosphatasesMultidisciplinaryAqueous solutionMolecular StructurePhysicsElectromagnetic RadiationHydrolysisRecombinant ProteinsMitochondriaChemistryMonomerOncologyBiochemistryPhysical SciencesInterdisciplinary PhysicsHSP60Research ArticleProtein BindingProtein Structureanimal structuresBiophysicschemical and pharmacologic phenomenaBiologycomplex mixturesMitochondrial ProteinsHumansProtein InteractionsMolecular BiologyInflammationChemical PhysicsCell-Free Systemlcsh:RfungiLight ScatteringBiology and Life SciencesProteinsProtein ComplexesChaperonin 60Chaperone ProteinsCytosolSpectrometry FluorescencechemistryMolecular Complexeslcsh:QPLoS ONE
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De Novo Mutations in SLC25A24 Cause a Disorder Characterized by Early Aging, Bone Dysplasia, Characteristic Face, and Early Demise

2017

International audience; A series of simplex cases have been reported under various diagnoses sharing early aging, especially evident in congenitally decreased subcutaneous fat tissue and sparse hair, bone dysplasia of the skull and fingers, a distinctive facial gestalt, and prenatal and postnatal growth retardation. For historical reasons, we suggest naming the entity Fontaine syndrome. Exome sequencing of four unrelated affected individuals showed that all carried the de novo missense variant c.649C>T (p.Arg217Cys) or c.650G>A (p.Arg217His) in SLC25A24, a solute carrier 25 family member coding for calcium-binding mitochondrial carrier protein (SCaMC-1, also known as SLC25A24). SLC25A24 all…

Male0301 basic medicineAgingMitochondrionPetty syndromeAntiportersATP-Mg/Pi carriersAdenosine TriphosphateCytosol0302 clinical medicineAdenine nucleotideMissense mutation[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human geneticsGenetics (clinical)Exome sequencingMembrane Potential MitochondrialGeneticsProgeriaATP synthaseSCaMC-1SyndromeMitochondria3. Good healthFemalemedicine.medical_specialtylipodystrophyMolecular Dynamics SimulationBiologyPhosphatesMitochondrial Proteins03 medical and health sciencesReportInternal medicineGeneticsmedicineHumansFetal DeathBone Diseases DevelopmentalAdenineSLC25A24Calcium-Binding ProteinsagingInfant NewbornInfantprogeriaFibroblastsmedicine.diseaseMitochondrial carrierSolute carrier familyOxygenprogeroid disorder030104 developmental biologyEndocrinology[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsMutationbiology.protein030217 neurology & neurosurgery
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