Search results for "Zinc Fingers"

showing 10 items of 21 documents

Mutations in a new gene, encoding a zinc-finger protein, cause tricho-rhino-phalangeal syndrome type I

1999

Tricho-rhino-phalangeal syndrome type I (TRPS I, MIM 190350) is a malformation syndrome characterized by craniofacial and skeletal abnormalities and is inherited in an autosomal dominant manner. TRPS I patients have sparse scalp hair, a bulbous tip of the nose, a long flat philtrum, a thin upper vermilion border and protruding ears. Skeletal abnormalities include cone-shaped epiphyses at the phalanges, hip malformations and short stature. We assigned TRPS1 to human chromosome 8q24. It maps proximal of EXT1, which is affected in a subgroup of patients with multiple cartilaginous exostoses and deleted in all patients with TRPS type II (TRPS II, or Langer-Giedion syndrome, MIM 150230; ref.2-5)…

MaleDNA Complementaryanimal structuresLanger-Giedion SyndromeMolecular Sequence DataBiologyLanger–Giedion syndromeOpen Reading FramesTRPS1 geneotorhinolaryngologic diseasesGeneticsmedicineTricho–rhino–phalangeal syndromeHumansGeneZinc fingerGeneticsSyndrome typeChromosome MappingZinc Fingersmedicine.diseaseBlotting NorthernPedigreeTrichorhinophalangeal syndromeMutationTrichorhinophalangeal Syndrome Type IFemaleChromosomes Human Pair 8Nature genetics
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Nuclear localization of the protein encoded by the Wilms’ tumor gene WT1 in embryonic and adult tissues

1993

ABSTRACT The human Wilms’ tumor gene WT1 encodes a putative transcription factor implicated in tumorigenesis and in specifying normal urogenital development. We have studied the distribution of WT1 protein and mRNA using immunohistochemistry and in situ hybridization. Monoclonal antibodies were raised against a peptide specific to the first alternative splice site of WT1. Two antibodies specifically reacted on Western blot to this WT1 isoform. Immunofluorescence localized WT1 protein to podocytes during mesonephric and metanephric development. In situ hybridization revealed a similar pattern of expression except that WT1 mRNA was also present in metanephric blastema and renal vesicles. Mess…

MaleGene isoformcongenital hereditary and neonatal diseases and abnormalitiesmedicine.medical_specialtyBlotting WesternFluorescent Antibody TechniqueGene ExpressionUrogenital SystemIn situ hybridizationBiologyKidneyurologic and male genital diseasesPolymerase Chain ReactionInternal medicineGene expressionmedicineHumansRNA MessengerWT1 ProteinsMolecular BiologyTranscription factorIn Situ HybridizationCell NucleusMessenger RNAGranulosa CellsSertoli Cellsurogenital systemfungiZinc FingersWilms' tumormedicine.diseasefemale genital diseases and pregnancy complicationsWilms Tumor ProteinCell biologyDNA-Binding ProteinsCell nucleusmedicine.anatomical_structureEndocrinologyMesonephrosFemaleTranscription FactorsDevelopmental BiologyDevelopment
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Cyclometalated Au(III) Complexes for Cysteine Arylation in Zinc Finger Protein Domains: Towards Controlled Reductive Elimination

2019

With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C-atom transfer, the gold-mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCON)Cl2] complex featuring the 2-benzoylpyridine (CCON) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high-resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (Q…

Models Molecularzinc finger proteinProtein DomainPeptidecatalysi010402 general chemistry01 natural sciencesCatalysisReductive eliminationCatalysisThermodynamicOrganogold Compounds[CHIM]Chemical SciencesReactivity (chemistry)CysteineZinc fingerchemistry.chemical_classificationAqueous solutionCoordination Complexe010405 organic chemistryOrganic Chemistryreductive eliminationZinc FingersGeneral ChemistryCombinatorial chemistry0104 chemical sciencescysteine arylationchemistrySettore CHIM/03 - Chimica Generale E Inorganicagold complexeQuantum TheoryGoldCysteine
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Conserved Structure and Promoter Sequence Similarity in the Mouse and Human Genes Encoding the Zinc Finger Factor BERF-1/BFCOL1/ZBP-89

2001

Abstract We have characterized the genomic structure of the mouse Zfp148 gene encoding Beta-Enolase Repressor Factor-1 (BERF-1), a Kruppel-like zinc finger protein involved in the transcriptional regulation of several genes, which is also termed ZBP-89, BFCOL1. The cloned Zfp148 gene spans 110 kb of genomic DNA encompassing the 5′-end region, 9 exons, 8 introns, and the 3′-untranslated region. The promoter region displays the typical features of a housekeeping gene: a high G+C content and the absence of canonical TATA and CAAT boxes consistent with the multiple transcription initiation sites determined by primary extension analysis. Computer-assisted search in the human genome database allo…

Molecular Sequence DataResponse elementBiophysicsCodon InitiatorRegulatory Sequences Nucleic AcidBiologyBiochemistryConserved non-coding sequenceMiceExonAnimalsHumansPromoter Regions GeneticMolecular BiologyGeneConserved SequenceGeneticsZinc fingerBase SequenceAlternative splicingIntronZinc FingersPromoterExonsCell BiologyIntronsDNA-Binding ProteinsAlternative Splicing5' Untranslated RegionsTranscription FactorsBiochemical and Biophysical Research Communications
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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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Cyclic AMP-induced Chromatin Changes Support the NFATc-mediated Recruitment of GATA-3 to the Interleukin 5 Promoter

2008

Elevated intracellular cyclic AMP levels, which suppress the proliferation of naive T cells and type 1 T helper (Th1) cells are a property of T helper 2 (Th2) cells and regulatory T cells. While cyclic AMP signals interfere with the IL-2 promoter induction, they support the induction of Th2-type genes, in particular of il-5 gene. We show here that cyclic AMP signals support the generation of three inducible DNase I hypersensitive chromatin sites over the il-5 locus, including its promoter region. In addition, cyclic AMP signals enhance histone H3 acetylation at the IL-5 promoter and the concerted binding of GATA-3 and NFATc to the promoter. This is facilitated by direct protein-protein inte…

Quantitative Trait LociGATA3 Transcription FactorBiologyBiochemistryCell LineHistonesMiceTh2 CellsCyclic AMPTranscriptional regulationAnimalsHumansTranscription Chromatin and EpigeneticsPromoter Regions GeneticHistone H3 acetylationMolecular BiologyInterleukin 5Cell ProliferationMice Inbred BALB CNFATC Transcription FactorsEffectorLymphokineAcetylationZinc FingersPromoterCell BiologyDNA-binding domainTh1 CellsChromatin Assembly and DisassemblyMolecular biologyChromatinProtein Structure TertiaryChromatinGene Expression RegulationInterleukin-2Interleukin-5Signal TransductionJournal of Biological Chemistry
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The differentiation of the serotonergic neurons in the Drosophila ventral nerve cord depends on the combined function of the zinc finger proteins Eag…

1997

ABSTRACT The Drosophila ventral nerve cord (vNC) derives from a stereotyped population of neural stem cells, neuroblasts (NBs), each of which gives rise to a characteristic cell lineage. The mechanisms leading to the specification and differentiation of these lineages are largely unknown. Here we analyse mechanisms leading to cell differentiation within the NB 7-3 lineage. Analogous to the grasshopper, NB 7-3 is the progenitor of the Drosophila vNC serotonergic neurons. The zinc finger protein Eagle (Eg) is expressed in NB 7-3 just after delamination and is present in all NB 7-3 progeny until late stage 17. DiI cell lineage tracing and immunocytochemistry reveal that eg is required for norm…

Receptors SteroidSerotoninDopamineCellular differentiationBiologyCell fate determinationNervous SystemNeuroblastAbdomenAnimalsDrosophila ProteinsCell LineageProgenitor cellMolecular BiologyIn Situ HybridizationNeuronsZinc fingerStem CellsNeuropeptidesGene Expression Regulation DevelopmentalCell DifferentiationZinc FingersAnatomyImmunohistochemistryengrailedCell biologyDNA-Binding ProteinsSegment polarity geneDrosophilaEctopic expressionDevelopmental BiologyDevelopment
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The yeast putative transcriptional repressor RGM1 is a proline-rich zinc finger protein.

1991

Abstract I have cloned a yeast gene, RGM1, which encodes a proline-rich zinc, finger protein. rgm1 mutants do not show any obvious phenotype but overexpression of RGM1 gene greatly impairs cell growth. The proline-rich region of RGM1 attached to a heterologous DNA binding domain is able to repress the expression of the target gene. RGM1 shares similar zinc finger motifs with the mammalian Egr (early growth response) proteins as well as proline-rich sequences with a high serine and threonine content, suggesting that RGM1 and Egr proteins could have functional similarities.

Recombinant Fusion ProteinsMolecular Sequence DataRestriction MappingGene ExpressionSaccharomyces cerevisiaeBiologyZIC2TransfectionSequence Homology Nucleic AcidGene expressionGeneticsAmino Acid SequenceCloning MolecularLIM domainSIN3BZinc fingerBase SequenceZinc FingersDNA-binding domainZinc finger nucleaseRING finger domainbody regionsRepressor ProteinsBiochemistryMutagenesisCarbohydrate MetabolismPlasmidsNucleic acids research
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ZFWD: a novel subfamily of plant proteins containing a C3H zinc finger and seven WD40 repeats

2000

We describe a new subfamily of WD repeat proteins characterised by the presence of a C3H zinc finger at the N-terminal part of the protein associated with seven WD40 repeats. We have identified four members of this subfamily in Arabidopsis thaliana, one of them with associated expressed sequence tags (ESTs). We have also identified homologous ESTs in rice, cotton, maize, poplar, pine tree and the ice plant. We do not observe animal homologues, suggesting that this subfamily could be specific for plants. Our data suggest an important role for these proteins. Based on the high sequence conservation within the conserved domains, we suggest that these proteins could have a regulatory function.

Repetitive Sequences Amino AcidDNA ComplementarySubfamilyDNA PlantMolecular Sequence DataArabidopsisSequence alignmentBiologyEvolution MolecularWD40 repeatGeneticsProtein IsoformsArabidopsis thalianaAmino Acid SequencePeptide sequencePhylogenyPlant ProteinsExpressed Sequence TagsGeneticsZinc fingerExpressed sequence tagProtein subfamilySequence Homology Amino AcidArabidopsis Proteinsfungifood and beveragesZinc FingersSequence Analysis DNAGeneral Medicinebiology.organism_classificationSequence AlignmentGene
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Regulation of mating in the budding yeast Saccharomyces cerevisiae by the zinc cluster proteins Sut1 and Sut2

2013

This article is made available through the Brunel Open Access Publishing Fund. Copyright @ The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The zinc cluster proteins Sut1 and Sut2 play a role in sterol uptake and filamentous growth in the budding yeast Saccharomyces cerevisiae. In this study, we show that they are also involved in mating. Cells that lack both SUT1 and SUT2 were defective in mating. The expression of the genes NCE102 and PRR2 was increased in the sut1 sut2 double deletion mutant…

Saccharomyces cerevisiae ProteinsMonosaccharide Transport ProteinsSaccharomyces cerevisiaeBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryFungal ProteinsGene Expression Regulation FungalReproduction AsexualBudding yeastMatingMolecular BiologyGenereproductive and urinary physiologyGeneticsMatingZinc FingersCell Biologybiology.organism_classificationBudding yeastSut2Sut1Mating of yeastPheromone responseZinc cluster proteinsZinc Clusterbehavior and behavior mechanismsPheromoneTranscription FactorsSterol uptakeBiochemical and Biophysical Research Communications
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