Search results for "Selenocysteine"

showing 10 items of 10 documents

Cysteine, glutathione and a new genetic code: biochemical adaptations of the primordial cells that spread into open water and survived biospheric oxy…

2019

Abstract Life most likely developed under hyperthermic and anaerobic conditions in close vicinity to a stable geochemical source of energy. Epitomizing this conception, the first cells may have arisen in submarine hydrothermal vents in the middle of a gradient established by the hot and alkaline hydrothermal fluid and the cooler and more acidic water of the ocean. To enable their escape from this energy-providing gradient layer, the early cells must have overcome a whole series of obstacles. Beyond the loss of their energy source, the early cells had to adapt to a loss of external iron-sulfur catalysis as well as to a formidable temperature drop. The developed solutions to these two problem…

0301 basic medicineClinical BiochemistryBiochemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCysteineMolecular Biologychemistry.chemical_classificationMethionineSelenocysteinebiologyWaterGlutathionebiology.organism_classificationAdaptation PhysiologicalGlutathioneAmino acidOxygen030104 developmental biologychemistryGenetic CodeBiophysicsEnergy source030217 neurology & neurosurgeryCysteineArchaeaHydrothermal ventBiological Chemistry
researchProduct

Modern diversification of the amino acid repertoire driven by oxygen

2017

All extant life employs the same 20 amino acids for protein biosynthesis. Studies on the number of amino acids necessary to produce a foldable and catalytically active polypeptide have shown that a basis set of 7-13 amino acids is sufficient to build major structural elements of modern proteins. Hence, the reasons for the evolutionary selection of the current 20 amino acids out of a much larger available pool have remained elusive. Here, we have analyzed the quantum chemistry of all proteinogenic and various prebiotic amino acids. We find that the energetic HOMO-LUMO gap, a correlate of chemical reactivity, becomes incrementally closer in modern amino acids, reaching the level of specialize…

0301 basic medicinechemistry.chemical_classificationMultidisciplinarySelenocysteineChemistryRadicalOrigin of LifeTryptophanGenetic codeAmino acidOxygen03 medical and health scienceschemistry.chemical_compound030104 developmental biologyModels ChemicalBiochemistryAbiogenesisPhysical SciencesProtein biosynthesisAmino AcidsTyrosineProceedings of the National Academy of Sciences
researchProduct

Gene Amplification-Associated Overexpression of the Selenoprotein tRNA Enzyme TRIT1 Confers Sensitivity to Arsenic Trioxide in Small-Cell Lung Cancer

2021

Simple Summary Small-cell lung cancer accounts for approximately 13% of all new lung cancer diagnoses, but in contrast to non-small-cell lung cancer, the implementation of targeted treatments in small-cell lung cancer has been limited, with little improvement in the clinical outcome in the last several decades. Exploring new pathways for targeted therapy, we have observed that extra-copies of the tRNA modifier TRIT1, involved in the translation of selenoproteins, confers sensitivity to arsenic trioxide in small-cell lung cancer. This finding could open a new therapeutic niche for a tumor type with such a dismal clinical course. The alteration of RNA modification patterns is emerging as a co…

Cancer Researchgene amplificationCellTRIT1lcsh:RC254-282Articlechemistry.chemical_compoundRNA modificationsGene duplicationmedicinesmall-cell lung cancerArsenic trioxideGenechemistry.chemical_classificationSelenocysteineChemistryRNAlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogenstransfer RNACell biologymedicine.anatomical_structureOncologyTransfer RNAselenoproteinsCàncer de pulmóRNASelenoproteinLung cancer
researchProduct

Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities.

2011

Reactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explor…

GPX1AntioxidantPhysiologyProtein Conformationmedicine.medical_treatmentClinical BiochemistryMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeBiochemistryDiabetes mellitus geneticschemistry.chemical_compoundGlutathione Peroxidase GPX1Risk FactorsComprehensive Invited ReviewNeoplasmsmedicineDiabetes MellitusAnimalsHumansGenetic Predisposition to DiseaseAmino Acid SequenceEnzyme InhibitorsHydrogen peroxideMolecular BiologyGeneral Environmental Sciencechemistry.chemical_classificationReactive oxygen speciesGlutathione PeroxidasePolymorphism GeneticCell DeathSuperoxideCell BiologyGlutathioneSelenocysteineOxidative StresschemistryBiochemistryGene Expression RegulationCardiovascular DiseasesGeneral Earth and Planetary SciencesReactive Oxygen SpeciesOxidation-ReductionOxidative stressAntioxidantsredox signaling
researchProduct

The Effect of tRNA

2021

Transfer RNA[Ser]Sec carries multiple post-transcriptional modifications. The A37G mutation in tRNA[Ser]Sec abrogates isopentenylation of base 37 and has a profound effect on selenoprotein expression in mice. Patients with a homozygous pathogenic p.R323Q variant in tRNA-isopentenyl-transferase (TRIT1) show a severe neurological disorder, and hence we wondered whether selenoprotein expression was impaired. Patient fibroblasts with the homozygous p.R323Q variant did not show a general decrease in selenoprotein expression. However, recombinant human TRIT1R323Q had significantly diminished activities towards several tRNA substrates in vitro. We thus engineered mice conditionally deficient in Tr…

GPX1medicine.disease_causelaw.inventiontRNA<sup>[Ser]Sec</sup>MiceRNA TransferlawBiology (General)Trit1Selenoproteins<i>Trit1</i>Spectroscopychemistry.chemical_classificationNeuronsMutationChemistryTranslation (biology)General MedicineComputer Science ApplicationsBlotChemistryLiverTransfer RNARecombinant DNAQH301-705.5isopentenylationCatalysisArticleCell LineInorganic ChemistrySeleniumSelenoprotein PmedicineAnimalsHumansCysteinePhysical and Theoretical ChemistrytRNA[Ser]SecMolecular BiologyQD1-999Alkyl and Aryl TransferasesOrganic ChemistryPhosphotransferasesMolecular biologyIn vitroSelenocysteineProtein BiosynthesisHepatocytesSelenoproteinRibosomesInternational journal of molecular sciences
researchProduct

A bioinformatical approach suggests the function of the autoimmune hepatitis target antigen soluble liver antigen/liver pancreas

2001

Antibodies to a soluble liver antigen/liver pancreas (SLA/LP) appear to be highly specific for the diagnosis of autoimmune hepatitis. The SLA/LP target antigen was recently identified as a hitherto unknown gene encoding 474 amino acid residues. The function of this antigen remains unclear, because it does not share sequence homology with proteins of known function stored in any of the publicly accessible databases. Therefore we used a new theoretical method called fold recognition and could show that the SLA/LP sequence is compatible with the architecture of the superfamily of pyridoxal phosphate (PLP; vitamin B6)-dependent transferases. Its function is likely to be that of a serine hydroxy…

Models MolecularAutoimmune diseaseHepatitisHepatologySelenocysteineMolecular Sequence DataComputational BiologyAutoimmune hepatitisBiologymedicine.diseaseAutoantigensHepatitis Autoimmunechemistry.chemical_compoundchemistryBiochemistryAntigenSerine hydroxymethyltransferasebiology.proteinmedicineHumansAmino Acid SequenceAntibodyPyridoxal phosphateHepatology
researchProduct

Reactivity of antitumor coinage metal-based N-heterocyclic carbene complexes with cysteine and selenocysteine protein sites

2021

Abstract The reaction of the antitumor M(I)-bis-N-heterocyclic carbene (M(I)-NHC) complexes, M = Cu, Ag, and Au, with their potential protein binding sites, i.e. cysteine and selenocysteine, was investigated by means of density functional theory approaches. Capped cysteine and selenocysteine were employed to better model the corresponding residues environment within peptide structures. By assuming the neutral or deprotonated form of the side chains of these amino acids and by considering the possible assistance of an external proton donor such as an adjacent acidic residue or the acidic component of the surrounding buffer environment, we devised five possible routes leading to the binding o…

SilverAnticancer; Copper(I) complexes; DFT calculations; Gold(I) complexes; N-heterocyclic carbenes; Silver(I) complexesStereochemistryCoinage metalsAntineoplastic AgentsProtonationLigandsDFT calculationsBiochemistrySilver(I) complexesInorganic Chemistrychemistry.chemical_compoundDeprotonationProtein structureCoordination ComplexesCysteineN-heterocyclic carbenesDensity Functional Theorychemistry.chemical_classificationMolecular StructureSelenocysteineCopper(I) complexesSelenocysteineAmino acidAnticancerGold(I) complexesModels ChemicalchemistryThermodynamicsGoldCarbeneCopperCysteineJournal of Inorganic Biochemistry
researchProduct

Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
researchProduct

New Gold(I) Organometallic Compounds with Biological Activity in Cancer Cells

2014

N-Heterocyclic carbene gold(I) complexes bearing a fluorescent coumarin ligand were synthesized and characterized by various techniques. The compounds were examined for their antiproliferative effects in normal and tumor cells in vitro; they demonstrated moderate activity and a certain degree of selectivity. The compounds were also shown to efficiently inhibit the selenoenzyme thioredoxin reductase (TrxR), whereas they were poorly effective towards the glutathione reductase (GR) and glutathione peroxidase enzymes. Notably, {3-[(7-methoxy-2-oxo-2H-chromen-4-yl) methyl]-1-methylimidazol-2-ylidene}(tetra-O-acetyl-1-thio-beta-D-glucopyranosido) gold(I) (3) showed a pronounced inhibition of TrxR…

Thioredoxin reductaseGlutathione reductaseMECHANISMSInorganic Chemistrychemistry.chemical_compoundCoumarinsCHEMISTRYTARGETSN-HETEROCYCLIC CARBENESCancerchemistry.chemical_classificationSelenocysteineGlutathione peroxidaseGold; carbenes; coumarins; enzyme; CancerBiological activityLigand (biochemistry)EnzymesenzymechemistryBiochemistryCancer cellIodoacetamideCarbenesANTICANCER AGENTSCOMPLEXESGold
researchProduct

Selenoproteins, cholesterol-lowering drugs, and the consequences: revisiting of the mevalonate pathway.

2004

3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) and peroxisome proliferator-activated receptor alpha activators (fibrates) are the backbone of pharmacologic hypercholesterolemia and dyslipidemia treatment. Many of their clinical effects, however, are still enigmatic. This article describes how a side road of the mevalonate pathway, characterized in recent years, can rationalize a major fraction of these unexplained observations. This side road is the enzymatic isopentenylation of selenocysteine-tRNA([Ser]Sec) (Sec-tRNA), the singular tRNA to decode the unusual amino acid selenocysteine. The functionally indispensable isopentenylation of Sec-tRNA requires a unique interm…

chemistry.chemical_classificationSelenocysteineCoenzyme AHypercholesterolemiaPeroxisome Proliferator-Activated ReceptorsIsopentenyl pyrophosphateMevalonic AcidProteinsBiologyPeroxisomeRNA Transfer Amino AcylAmino acidchemistry.chemical_compoundEnzymechemistryBiochemistryAnimalsMevalonate pathwaySelenoproteinHydroxymethylglutaryl-CoA Reductase InhibitorsCardiology and Cardiovascular MedicineSelenoproteinsTrends in cardiovascular medicine
researchProduct