Search results for "SUBUNIT"

showing 10 items of 513 documents

Data from: Cuticular hydrocarbons as potential mediators of cryptic species divergence in a mutualistic ant association

2019

Upon advances in sequencing techniques, more and more morphologically identical organisms are identified as cryptic species. Often, mutualistic interactions are proposed as drivers of diversification. Species of the Neotropical parabiotic ant association between Crematogaster levior and Camponotus femoratus are known for highly diverse cuticular hydrocarbon (CHC) profiles, which in insects serve as desiccation barrier but also as communication cues. In the present study we investigated the association of the ants’ CHC profiles to genotypes and morphological traits, and discovered cryptic species pairs in both genera. To assess putative niche differentiation between the cryptic species, we c…

Crematogaster leviorcytochrome c oxidase subunit ICamponotus femoratusBarcoding
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Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy

1994

Human hepatitis B virus core protein expressed in E. coli assembles into two sizes of particle. We have determined their three-dimensional structures by electron cryomicroscopy and image processing. The large and small particles correspond to triangulation number T = 4 and T = 3 dimer clustered packings, containing 240 and 180 protein subunits, respectively. The local packing of subunits is very similar in the two sizes of particle and shows holes or channels through the shell. The native viral core particle packages RNA and is active in reverse transcription to DNA. The holes we observe may provide access for the necessary small molecules. Shells assembled from the intact core protein cont…

CryopreservationHepatitis B virusProtein ConformationCryo-electron microscopyProtein subunitDimerShell (structure)RNABiologyHepatitis B Core AntigensVirologyRecombinant ProteinsGeneral Biochemistry Genetics and Molecular BiologyMicroscopy Electronchemistry.chemical_compoundCrystallographyProtein structurechemistryEscherichia coliImage Processing Computer-AssistedHumansParticleDNACell
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Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

1984

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drugBiochemical and Biophysical Research Communications
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A genetic approach to dissect the role of prefoldins in Arabidopsis

2021

SummaryThe prefoldin complex (PFDc) was identified in humans as co-chaperone of the cytosolic chaperonin TRiC/CCT. It is conserved in eukaryotes and is composed of subunits PFD1 to 6. PFDc-TRiC/CCT operates folding actin and tubulins. In addition to this function, PFDs participate in a wide range of cellular processes, both in the cytoplasm and in the nucleus, and their malfunction cause developmental alterations and disease in animals, and altered growth and environmental responses in yeast and plants. Genetic analyses in yeast indicate that not all functions performed by PFDs require the participation of the canonical complex. The lack of systematic genetic analyses in higher eukaryotes m…

CytoplasmProtein subunitArabidopsisMutantBiologyPrefoldin complexbiology.organism_classificationTranscription factorActinFunction (biology)Cell biology
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Analysis of cytochrome C oxidase subunits III and IV expression in developing rat brain

2004

Abstract Cytochrome c oxidase (COX) complex is built up with both nucleus- and mitochondrion-encoded subunits. Biogenesis and assembly of the complex thus requires fine cross-talk between the two compartments. In order to shed light on the regulation of nuclear–mitochondrial interactions, we studied the expression of COXIII (mitochondrion-encoded) and COXIV (nucleus-encoded) in adult rat tissues and rat developing brain. We found that the levels of COXIV protein and mRNA are not linearly related, thus suggesting a post-transcriptional mode of regulation. In agreement with this observation, we report the presence of a protein that specifically binds to the 3′-untranslated region of COXIV mRN…

CytoplasmRNA-binding proteinProtein subunitBlotting WesternCOX IVRNA-binding proteinMitochondrionBiologyGene Expression Regulation EnzymologicElectron Transport Complex IVAnimalsCytochrome c oxidaseElectrophoresis Gel Two-DimensionalCOX III.RNA MessengerRNA Processing Post-TranscriptionalMessenger RNAGeneral NeuroscienceBrainProteinsRNABlotting NorthernMitochondriaRatsProtein TransportCytosolnucleus-mitochondrion cross-talkBiochemistryCytoplasmbiology.proteinNeuroscience
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Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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Cutting edge: priming of CTL by transcutaneous peptide immunization with imiquimod.

2005

Abstract CTL are important in combating cancer and viruses. Therefore, triggering the complete potential of CTL effector functions by new vaccination strategies will not only improve prophylaxis of tumor or virus-related diseases, but also open opportunities for effective therapeutic immunizations. Using transcutaneous immunization, we show that epicutaneous (e.c.)4 application of an ointment containing a CTL epitope and the TLR7 ligand imiquimod is highly effective in activating T cells in mice using TCR-transgenic CTL or in wild-type mice. Transcutaneous immunization-activated CTL mount a full-blown immune response against the target epitope characterized by proliferation, cytolytic activ…

Cytotoxicity ImmunologicAdoptive cell transferImmunologyReceptors Antigen T-CellPriming (immunology)Epitopes T-Lymphocytechemical and pharmacologic phenomenaImiquimodMice TransgenicAdministration CutaneousLymphocyte ActivationResting Phase Cell CycleEpitopeMiceImmune systemmedicineImmunology and AllergyAnimalsCells CulturedMice KnockoutImiquimodbusiness.industryTLR7VirologyAdoptive TransferVaccinationMice Inbred C57BLCTL*Protein TransportImmunologyVaccines SubunitAminoquinolinesLymph NodesbusinessSpleenmedicine.drugT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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Impaired Transporter Associated with Antigen Processing (TAP) Function Attributable to a Single Amino Acid Alteration in the Peptide TAP Subunit TAP1

2003

Abstract The heterodimeric peptide transporter TAP belongs to the ABC transporter family. Sequence comparisons with the P-glycoprotein and cystic fibrosis transmembrane conductance regulator and the functional properties of selective amino acids in these ABC transporters postulated that the glutamic acid at position 263 and the phenylalanine at position 265 of the TAP1 subunit could affect peptide transporter function. To define the role of both amino acids, TAP1 mutants containing a deletion or a substitution to alanine at position 263 or 265 were generated and stably expressed in murine and human TAP1−/− cells. The different TAP1 mutants were characterized in terms of expression and funct…

Cytotoxicity ImmunologicMacromolecular SubstancesPhenylalanineImmunologyAntigen presentationGlutamic AcidATP-binding cassette transporterEndoplasmic ReticulumTransfectionCell LineMiceAdenosine TriphosphateATP Binding Cassette Transporter Subfamily B Member 3MHC class IAnimalsHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Sequence DeletionAlaninechemistry.chemical_classificationAntigen PresentationbiologyHistocompatibility Antigens Class I3T3 CellsIntracellular MembranesTransporter associated with antigen processingMolecular biologyPeptide FragmentsCystic fibrosis transmembrane conductance regulatorAmino acidMice Inbred C57BLProtein SubunitsAmino Acid SubstitutionBiochemistrychemistryMutagenesis Site-Directedbiology.proteinATP-Binding Cassette TransportersTAP1Sequence AlignmentProtein BindingT-Lymphocytes CytotoxicThe Journal of Immunology
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Class 1 Histone Deacetylases and Ataxia-Telangiectasia Mutated Kinase Control the Survival of Murine Pancreatic Cancer Cells upon dNTP Depletion

2021

Pancreatic ductal adenocarcinoma (PDAC) is a highly aggressive disease with a dismal prognosis. Here, we show how an inhibition of de novo dNTP synthesis by the ribonucleotide reductase (RNR) inhibitor hydroxyurea and an inhibition of epigenetic modifiers of the histone deacetylase (HDAC) family affect short-term cultured primary murine PDAC cells. We used clinically relevant doses of hydroxyurea and the class 1 HDAC inhibitor entinostat. We analyzed the cells by flow cytometry and immunoblot. Regarding the induction of apoptosis and DNA replication stress, hydroxyurea and the novel RNR inhibitor COH29 are superior to the topoisomerase-1 inhibitor irinotecan which is used to treat PDAC. Ent…

DNA Replicationendocrine system diseasesDNA damagereplication stressQH301-705.5RNR Inhibitor COH29Antineoplastic AgentsCell Cycle ProteinsRNRAtaxia Telangiectasia Mutated ProteinsArticle03 medical and health scienceschemistry.chemical_compoundAtaxia TelangiectasiaMice0302 clinical medicineHDACAnimalscancerPDAC cellsRibonucleotide Reductase SubunitEnzyme InhibitorsBiology (General)030304 developmental biology0303 health sciencesbiologyChemistryEntinostatDNA replicationapoptosisGeneral Medicine3. Good healthPancreatic NeoplasmsHistoneRibonucleotide reductase030220 oncology & carcinogenesisATMbiology.proteinCancer researchDNA damageHistone deacetylaseCells
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Identification of Gip as a novel phage‐encoded gyrase inhibitor protein of Corynebacterium glutamicum

2021

By targeting key regulatory hubs of their host, bacteriophages represent a powerful source for the identification of novel antimicrobial proteins. Here, a screening of small cytoplasmic proteins encoded by the CGP3 prophage of Corynebacterium glutamicum resulted in the identification of the gyrase-inhibiting protein Cg1978, termed Gip. Pull-down assays and surface plasmon resonance revealed a direct interaction of Gip with the gyrase subunit A (GyrA). The inhibitory activity of Gip was shown to be specific to the DNA gyrase of its bacterial host C. glutamicum. Overproduction of Gip in C. glutamicum resulted in a severe growth defect as well as an induction of the SOS response. Furthermore, …

DNA Replicationendocrine systemProtein subunitProphagesBiologyMicrobiologyDNA gyraseCorynebacterium glutamicum03 medical and health scienceschemistry.chemical_compoundViral Proteinsddc:570Topoisomerase II InhibitorsSOS responseMolecular BiologyProphage030304 developmental biology0303 health sciences030306 microbiologyDNA replicationAnti-Bacterial AgentsHigh-Throughput Screening AssaysCorynebacterium glutamicumchemistryBiochemistrybacteriaTopoisomerase-II InhibitorDNAhormones hormone substitutes and hormone antagonistsMolecular Microbiology
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