Search results for "DNA-BINDING PROTEIN"

showing 10 items of 449 documents

Cisplatin-induced apoptosis in 43-3B and 27-1 cells defective in nucleotide excision repair

2001

Cisplatin is a highly potent cytotoxic and genotoxic agent used in the chemotherapy of various types of tumors. Its cytotoxic effect is supposed to be due to the induction of intra- and interstrand DNA cross-links which are repaired via the nucleotide excision repair (NER) pathway. Here, we elucidated the mechanism of cisplatin-induced cytotoxicity in mutants derived from CHO-9 cells defective in NER. We compared 43-3B and 27-1 cells deficient for ERCC1 and ERCC3, respectively, with the corresponding wild-type and ERCC1 complemented 43-3B cells. It is shown that cells defective in ERCC1 are more sensitive than cells defective in ERCC3 with regard to cisplatin-induced reproductive cell death…

Programmed cell deathTime FactorsDNA RepairCell SurvivalPoly ADP ribose polymeraseBlotting WesternDown-RegulationApoptosisCHO CellsToxicologyCell LineNecrosisCricetinaeGeneticsmedicineAnimalsDrosophila ProteinsCytotoxic T cellMolecular BiologyCaspaseCisplatinCaspase 8Dose-Response Relationship DrugbiologyCaspase 3ProteinsEndonucleasesMolecular biologyCaspase 9DNA-Binding ProteinsEnzyme ActivationApoptosisCaspasesMutationbiology.proteinCancer researchCisplatinPoly(ADP-ribose) PolymerasesERCC1Nucleotide excision repairmedicine.drugMutation Research/DNA Repair
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Transmembrane BAX Inhibitor-1 Motif Containing Protein 5 (TMBIM5) Sustains Mitochondrial Structure, Shape, and Function by Impacting the Mitochondria…

2020

The Transmembrane Bax Inhibitor-1 motif (TMBIM)-containing protein family is evolutionarily conserved and has been implicated in cell death susceptibility. The only member with a mitochondrial localization is TMBIM5 (also known as GHITM or MICS1), which affects cristae organization and associates with the Parkinson&rsquo

Programmed cell deathmitochondrial metabolismProtein familyApoptosisMitochondrioncell survivalArticleGHITMMitochondrial ProteinsTMBIMHumansInner mitochondrial membranelcsh:QH301-705.5bcl-2-Associated X ProteinBAX inhibitor 1ChemistryMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyDNA-Binding Proteinsmitochondriacell deathMitochondrial biogenesislcsh:Biology (General)Mitochondrial Membranes
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Co-regulator recruitment and the mechanism of retinoic acid receptor synergy.

2002

Crystal structure and co-regulator interaction studies have led to a general mechanistic view of the initial steps of nuclear receptor (NR) action. Agonist-induced transconformation of the ligand-binding domain (holo-LBD) leads to the formation of co-activator complexes, and destabilizes the co-repressor complexes bound to the ligand-free (apo) LBD. However, the molecular basis of retinoid-X receptor (RXR) 'subordination' in heterodimers, an essential mechanism to avoid signalling pathway promiscuity, has remained elusive. RXR, in contrast to its heterodimer partner, cannot autonomously induce transcription on binding of cognate agonists. Here we show that RXR can bind ligand and recruit co…

Protein ConformationReceptors Retinoic AcidPlasma protein bindingRetinoid X receptorLigandsNuclear Receptor Coactivator 2Structure-Activity RelationshipmedicineNuclear Receptor Co-Repressor 2Binding siteNuclear receptor co-repressor 2PhysicsMultidisciplinaryCell biologyDNA-Binding ProteinsRepressor ProteinsRetinoic acid receptorRetinoid X ReceptorsMechanism of actionBiochemistryNuclear receptorModels Chemicalembryonic structuresNuclear receptor coactivator 2medicine.symptomDimerizationProtein BindingTranscription FactorsNature
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Interference by toxic metal ions with zinc-dependent proteins involved in maintaining genomic stability.

2002

Metal ions are essential components of biological systems; nevertheless, even essential elements may have toxic or carcinogenic properties. Thus, besides As(III) and Cd(II), also Ni(II) and Co(II) have been shown previously to disturb different types of DNA repair systems at low, non-cytotoxic concentrations. Since some metals exert high affinities for SH groups, we investigated whether zinc finger structures in DNA-binding motifs of DNA repair proteins are potential targets for toxic metal ions. The bacterial formamidopyrimidine-DNA glycosylase (Fpg protein) involved in base excision repair was inhibited by Cd(II), Cu(II) and Hg(II) with increasing efficiencies, whereas Co(II), As(III), Pb…

Protein FoldingDNA RepairDNA repairCations DivalentPoly ADP ribose polymeraseToxicologymedicine.disease_causechemistry.chemical_compoundMetals HeavymedicineMetallothioneinHumansN-Glycosyl HydrolasesChemistryRNA-Binding ProteinsZinc FingersGeneral MedicineBase excision repairXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinsZincBiochemistryDNA glycosylaseZinc toxicityDNAFood ScienceNucleotide excision repairFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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Proteins' Knotty Problems

2018

Abstract Knots in proteins are increasingly being recognized as an important structural concept, and the folding of these peculiar structures still poses considerable challenges. From a functional point of view, most protein knots discovered so far are either enzymes or DNA-binding proteins. Our comprehensive topological analysis of the Protein Data Bank reveals several novel structures including knotted mitochondrial proteins and the most deeply embedded protein knot discovered so far. For the latter, we propose a novel folding pathway based on the idea that a loose knot forms at a terminus and slides to its native position. For the mitochondrial proteins, we discuss the folding problem fr…

Protein FoldingProtein ConformationComputational biologyMitochondrial Proteins03 medical and health sciences0302 clinical medicineKnot (unit)Protein structurestomatognathic systemStructural BiologyHumansDatabases ProteinMolecular BiologyMitochondrial protein030304 developmental biologyPhysics0303 health sciencesMembrane Proteinsfood and beveragescomputer.file_formatProtein Data BankMitochondriaDNA-Binding Proteinssurgical procedures operativeMembrane proteincomputer030217 neurology & neurosurgeryJournal of Molecular Biology
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020

Abstract In the absence of sugars, C4-dicarboxylates (C4DC) like fumarate represent important substrates for growth of Escherichia coli. Aerobically, C4DCs are oxidized to CO2 whereas anaerobically, C4DCs are used for fumarate respiration. In order to determine the impact of fumarate under aerobic and anaerobic conditions, proteomes of E. coli W3110 grown aerobically or anaerobically with fumarate and/or the non-C4DC substrate glycerol were comparatively profiled by nanoLC-MS/MS. Membrane enrichment allowed sensitive detection of membrane proteins. A total of 1657 proteins of which 646 and 374 were assigned to the cytosol or membrane, respectively, were covered. Presence of fumarate trigger…

Proteomics0301 basic medicineBiophysicsCatabolite repressionmedicine.disease_causeBiochemistryCarbon utilization03 medical and health sciencesFumaratesTandem Mass SpectrometryEscherichia colimedicineDicarboxylic AcidsAnaerobiosisEscherichia coli030102 biochemistry & molecular biologybiologyChemistryEscherichia coli ProteinsGene Expression Regulation BacterialAerobiosisDNA-Binding ProteinsCitric acid cycle030104 developmental biologyRegulonMembrane proteinBiochemistrycAMP receptor proteinbiology.proteinProtein KinasesAnaerobic exerciseTranscription FactorsJournal of Proteomics
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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Changes in the proteome of sea urchin Paracentrotus lividus coelomocytes in response to LPS injection into the body cavity.

2020

Background The immune system of echinoderm sea urchins is characterised by a high degree of complexity that is not completely understood. The Mediterranean sea urchin Paracentrotus lividus coelomocytes mediate immune responses through phagocytosis, encapsulation of non-self particles, and production of diffusible factors including antimicrobial molecules. Details of these processes, and molecular pathways driving these mechanisms, are still to be fully elucidated. Principal findings In the present study we treated the sea urchin P. lividus with the bacterial lipopolysaccharide (LPS) and collected coelomocytes at different time-points (1, 3, 6 and 24 hours). We have shown, using label-free q…

ProteomicsLipopolysaccharidesProteomeHydrolasesBiochemistry0302 clinical medicineParacentrotusMedicine and Health SciencesSea urchinCoelomocyteImmune ResponseCytoskeleton0303 health sciencesPhagocytesMultidisciplinarybiologyChemistryQREukaryotaAnimal ModelsCell biologyEnzymesEchinodermExperimental Organism Systems030220 oncology & carcinogenesisProteomeParacentrotusMedicineProtein Interaction NetworksCellular Structures and OrganellesNetwork AnalysisResearch ArticleEchinodermsComputer and Information Sciencesfood.ingredientScienceImmunologyLipopolysaccharideEndocytosisResearch and Analysis MethodsParacentrotus lividusLymphatic System03 medical and health sciencesfoodPhagocytosisbiology.animalHeat shock proteinDNA-binding proteinsAnimalsProtein Interactions030304 developmental biologyPhagocytosiAnimalOrganismsBiology and Life SciencesProteinsCell Biologybiology.organism_classificationInvertebratesCytoskeletal ProteinsGuanosine TriphosphataseProtein-Protein InteractionsPhagocyteImmune SystemSea UrchinsAnimal StudiesEnzymologyParacentrotuPLoS ONE
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