Search results for "Motif"

showing 10 items of 290 documents

Epigenomic landscape of human colorectal cancer unveils an aberrant core of pan-cancer enhancers orchestrated by YAP/TAZ

2021

Cancer is characterized by pervasive epigenetic alterations with enhancer dysfunction orchestrating the aberrant cancer transcriptional programs and transcriptional dependencies. Here, we epigenetically characterize human colorectal cancer (CRC) using de novo chromatin state discovery on a library of different patient-derived organoids. By exploring this resource, we unveil a tumor-specific deregulated enhancerome that is cancer cell-intrinsic and independent of interpatient heterogeneity. We show that the transcriptional coactivators YAP/TAZ act as key regulators of the conserved CRC gained enhancers. The same YAP/TAZ-bound enhancers display active chromatin profiles across diverse human t…

0301 basic medicineOrganoidEpigenomicsTranscription FactorGeneral Physics and AstronomyColorectal NeoplasmAdaptor Proteins Signal Transducing; Colorectal Neoplasms; Gene Expression Regulation Neoplastic; Histone Code; Humans; Models Genetic; Organoids; RNA-Seq; Single-Cell Analysis; Trans-Activators; Transcription Factors; Tumor Cells Cultured; Enhancer Elements Genetic; Epigenesis GeneticEpigenesis Genetic0302 clinical medicineModelsAdaptor Proteins Signal Transducing Colorectal Neoplasms Gene Expression Regulation NeoplasticHistone Code Humans Models Genetic Organoids RNA-Seq Single-Cell Analysis Trans-Activators Transcription Factors Tumor Cells Cultured Enhancer Elements Genetic Epigenesis GeneticTumor Cells CulturedCancer genomicsHistone codeRNA-SeqEpigenomicsAdaptor Proteins Signal Transducing; Colorectal Neoplasms; Gene Expression Regulation Neoplastic; Histone Code; Humans; Models Genetic; Organoids; RNA-Seq; Single-Cell Analysis; Trans-Activators; Transcription Factors; Transcriptional Coactivator with PDZ-Binding Motif Proteins; Tumor Cells Cultured; YAP-Signaling Proteins; Enhancer Elements Genetic; Epigenesis GeneticMultidisciplinaryCulturedQAdaptor Proteins3. Good healthChromatinTumor CellsGene Expression Regulation NeoplasticHistone CodeOrganoidsSingle-Cell AnalysiEnhancer Elements GeneticTrans-Activator030220 oncology & carcinogenesisSingle-Cell AnalysisColorectal NeoplasmsHumanEnhancer ElementsScienceTumour heterogeneityBiologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesGeneticmedicineHumansEpigeneticsEnhancerTranscription factorAdaptor Proteins Signal TransducingNeoplasticModels GeneticSignal TransducingCancerYAP-Signaling ProteinsGeneral Chemistrymedicine.diseaseColorectal cancerdigestive system diseases030104 developmental biologyGene Expression RegulationTranscriptional Coactivator with PDZ-Binding Motif ProteinsCancer cellCancer researchTrans-ActivatorsEpigenesisTranscription Factors
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eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences

2017

Abstract eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by …

0301 basic medicinePeptidyl transferaseProlineCytoskeleton organizationAmino Acid MotifsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalSaccharomyces cerevisiaeBioinformaticsRibosomeGTP Phosphohydrolases03 medical and health sciences0302 clinical medicinePeptide Initiation FactorsGene Expression Regulation FungalGeneticsProtein biosynthesisHumansMolecular BiologyPolyproline helixBinding SitesbiologyRNA-Binding Proteinsbiology.organism_classificationStop codonCell biology030104 developmental biologybiology.proteinGenome FungalHydrophobic and Hydrophilic InteractionsRibosomesEIF5A030217 neurology & neurosurgeryProtein BindingNucleic Acids Research
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In vivo selection of heterotypically interacting transmembrane helices: Complementary helix surfaces, rather than conserved interaction motifs, drive…

2017

Single pass transmembrane proteins make up almost half of the whole transmembrane proteome. Contacts between such bitopic transmembrane proteins are common, and oligomerization of their single transmembrane helix is involved in triggering and regulation of signal transduction across cell membranes. In several recent analyses the distribution of amino acids at helix-helix contact sides has been analyzed, and e.g. a preference of amino acids with small side chains has been identified. Here we select amino acids, amino acid pairings and amino acid motifs, which mediate strong interactions of single-span transmembrane α-helices. Our analysis illustrates an architecture of TM helix dimers that i…

0301 basic medicineProtein Conformation alpha-HelicalDimerAmino Acid MotifsBiophysicsBiologyBiochemistryBordetella pertussisProtein Structure Secondary03 medical and health scienceschemistry.chemical_compoundAmino Acid SequenceAmino Acidschemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinAmino acidCrystallographyTransmembrane domain030104 developmental biologyMembrane proteinchemistryProteomeHelixBiophysicsProtein foldingDimerizationBiochimica et biophysica acta. Biomembranes
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Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues

2021

Abstract Post-translational modified thiazole–amino acid (Xaa–Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole–amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation; which is stabilised mainly by N–H⋯N…

0301 basic medicineStereochemistryClinical BiochemistryNon-standard amino acidsMolecular ConformationRamachandran map010402 general chemistryRing (chemistry)01 natural sciencesBiochemistryDFT03 medical and health scienceschemistry.chemical_compoundDehydroalanineAmino AcidsStructural motifThiazoleOxazoleAlaninechemistry.chemical_classificationHydrogen bondNon-standard amino AIDSHydrogen bondOrganic ChemistryHydrogen Bonding0104 chemical sciencesAmino acidThiazoles030104 developmental biologyConformational analysischemistryOriginal ArticleThiazolePeptidesAmino Acids
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The nucleic acid-binding protein PcCNBP is transcriptionally regulated during the immune response in red swamp crayfish Procambarus clarkii

2016

Gene family encoding cellular nucleic acid binding proteins (CNBP) is well conserved among vertebrates; however, there is limited knowledge in lower organisms. In this study, a CNBP homolog from the red swamp crayfish Procambarus clarkii was characterised. The full-length cDNA of PcCNBP was of 1257 bp with a 5′-untranslated region (UTR) of 63 bp and a 3′-UTR of 331 bp with a poly (A) tail, and an open-reading frame (ORF) of 864 bp encoding a polypeptide of 287 amino acids with the predicted molecular weight of about 33 kDa. The predicted protein possesses 7 tandem repeats of 14 amino acids containing the CCHC zinc finger consensus sequence, two RGG-rich single-stranded RNA-binding domain an…

0301 basic medicineUntranslated regionNucleic acid-binding proteinDNA ComplementaryHemocytesTranscription GeneticGene ExpressionHepatopancreasSettore BIO/11 - Biologia MolecolareAstacoideaBiochemistry03 medical and health sciencesComplementary DNAAnimalsGene expression patternTissue DistributionAmino Acid SequenceZinc finger motifsProcambarus clarkiiZinc fingerchemistry.chemical_classificationInnate immunityOriginal PaperbiologyRNA-Binding ProteinsMolecular Sequence AnnotationZinc finger motifCell Biologybiology.organism_classificationCrayfishMolecular biologyCrayfishImmunity InnateCell biologyAmino acid030104 developmental biologychemistryNucleic acidHepatopancreasCrayfish; Gene expression pattern; Innate immunity; Nucleic acid-binding protein; Zinc finger motifs; Biochemistry; Cell Biology
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Avoided motifs: short amino acid strings missing from protein datasets.

2020

Abstract According to the amino acid composition of natural proteins, it could be expected that all possible sequences of three or four amino acids will occur at least once in large protein datasets purely by chance. However, in some species or cellular context, specific short amino acid motifs are missing due to unknown reasons. We describe these as Avoided Motifs, short amino acid combinations missing from biological sequences. Here we identify 209 human and 154 bacterial Avoided Motifs of length four amino acids, and discuss their possible functionality according to their presence in other species. Furthermore, we determine two Avoided Motifs of length three amino acids in human proteins…

0301 basic medicinechemistry.chemical_classificationProtein functionAmino Acid Motifs030102 biochemistry & molecular biologyClinical BiochemistryComputational BiologyProteinsContext (language use)Computational biologyBiologyBiochemistryAmino acid03 medical and health sciences030104 developmental biologySecretory proteinchemistryAmino acid compositionCytoplasmMolecular BiologyHuman proteinsSequence AlignmentBiological chemistryReferences
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Characterization of sulfhydryl oxidase from Aspergillus tubingensis

2017

Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…

0301 basic medicineentsyymitBOVINE-MILKThioredoxin reductaselcsh:Animal biochemistryBiochemistrySubstrate Specificitychemistry.chemical_compoundNonribosomal peptide synthesisEnzyme Stabilitylcsh:QD415-436DisulfidesDISULFIDE BONDSPeptide Synthaseschemistry.chemical_classificationbiologyGliotoxinChemistrynonribosomal peptide synthesisHydrogen-Ion ConcentrationGlutathioneFAMILYSOXSglutathione oxidationhomesienetAspergillusBiochemistrySENSITIVITYsecreted sulfhydryl oxidaseOxidoreductasesResearch ArticleDithiol oxidaseCofactorlcsh:Biochemistry03 medical and health sciencesNonribosomal peptideNATURAL-PRODUCTSoksidoreduktaasitBIOSYNTHESISlcsh:QP501-801Molecular Biologysecondary metabolismPURIFICATIONIDENTIFICATION030102 biochemistry & molecular biologyCXXC-MOTIFGlutathioneNIGERluonnonaineet030104 developmental biologyEnzymedithiol oxidasebiology.protein1182 Biochemistry cell and molecular biologyAspergillus tubingensisSecreted sulfhydryl oxidaseSecondary metabolismGlutathione oxidationCysteineBMC Biochemistry
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Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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