Search results for "Eukaryotic Small Ribosomal Subunit"

showing 4 items of 4 documents

Characterization of two alternative Interleukin(IL)-10 5′UTR mRNA sequences, induced by lipopolysaccharide (LPS) stimulation of peripheral blood mono…

2009

Abstract IL-10 production shows a broad-spectrum of individual response, suggesting a genetic component of approximately 75%. Different polymorphisms located close to, or within the IL-10 gene has been demonstrated to influence its transcription rate whereas the post-transcriptional regulation of IL-10 production has not well elucidated. The main responsible elements at this control level are both the 5′- and 3′-untranslated regions (UTR's) of mRNAs, and as the 3′-UTR regions are mainly involved in the stability and decay rate of mRNAs, the 5′-UTR regions mediate the binding rate of the molecule with ribosomal 40S subunit as a cis-acting element. Herein are report data on the identification…

LipopolysaccharidesUntranslated regionFive prime untranslated regionmRNALPS stimulationMolecular Sequence DataImmunologyStimulationRegulatory Sequences Nucleic AcidBiologyPeripheral blood mononuclear cellInterleukin(IL)-10Secondary structureHumansEukaryotic Small Ribosomal SubunitRNA MessengerMolecular BiologyCells CulturedMessenger RNABase Sequence5′UTR regionInterleukinMolecular biologyInterleukin-10Interleukin 10Gene Expression RegulationLeukocytes MononuclearNucleic Acid Conformation5' Untranslated RegionsMolecular Immunology
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Partial Methylation at Am100 in 18S rRNA of Baker's Yeast Reveals Ribosome Heterogeneity on the Level of Eukaryotic rRNA Modification

2014

Ribosome heterogeneity is of increasing biological significance and several examples have been described for multicellular and single cells organisms. In here we show for the first time a variation in ribose methylation within the 18S rRNA of Saccharomyces cerevisiae. Using RNA-cleaving DNAzymes, we could specifically demonstrate that a significant amount of S. cerevisiae ribosomes are not methylated at 2'-O-ribose of A100 residue in the 18S rRNA. Furthermore, using LC-UV-MS/MS of a respective 18S rRNA fragment, we could not only corroborate the partial methylation at A100, but could also quantify the methylated versus non-methylated A100 residue. Here, we exhibit that only 68% of A100 in t…

Science5.8S ribosomal RNAYeast and Fungal ModelsSaccharomyces cerevisiaeMycologyBiologyMethylationBiochemistryMicrobiologyMolecular GeneticsModel OrganismsMolecular cell biologyRRNA modification23S ribosomal RNANucleic Acidsddc:570GeneticsEukaryotic Small Ribosomal SubunitBiologyNucleic Acid ComponentsGeneticsMultidisciplinaryQRTranslation (biology)DNAMethylationRibosomal RNAYeastRNA processingBiochemistryRNA RibosomalRibosome SubunitsMedicineRNARibosomesResearch ArticlePLoS ONE
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Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1-PP2A protein complex.

2012

Expansion of CAG repeats is a common feature of various neurodegenerative disorders, including Huntington's disease. Here we show that expanded CAG repeats bind to a translation regulatory protein complex containing MID1, protein phosphatase 2A and 40S ribosomal S6 kinase. Binding of the MID1-protein phosphatase 2A protein complex increases with CAG repeat size and stimulates translation of the CAG repeat expansion containing messenger RNA in a MID1-, protein phosphatase 2A- and mammalian target of rapamycin-dependent manner. Our data indicate that pathological CAG repeat expansions upregulate protein translation leading to an overproduction of aberrant protein and suggest that the MID1-com…

metabolism [Microtubule Proteins]General Physics and AstronomyHTT protein humanRibosomal s6 kinaseMice0302 clinical medicinemetabolism [Transcription Factors]Protein Phosphatase 2Luciferasesgenetics [Nerve Tissue Proteins]genetics [Protein Biosynthesis]0303 health sciencesHuntingtin ProteinMultidisciplinarybiologyTOR Serine-Threonine KinasesNuclear ProteinsTranslation (biology)3. Good healthmetabolism [Luciferases]Microtubule Proteinsddc:500metabolism [Nuclear Proteins]genetics [Trinucleotide Repeat Expansion]Protein Bindingcongenital hereditary and neonatal diseases and abnormalitiesMTOR protein humanUbiquitin-Protein LigasesBlotting WesternNerve Tissue Proteinsmetabolism [TOR Serine-Threonine Kinases]metabolism [RNA Messenger]General Biochemistry Genetics and Molecular Biology03 medical and health sciencesgenetics [RNA Messenger]mental disordersHuntingtin ProteinAnimalsHumansEukaryotic Small Ribosomal SubunitRNA MessengerNucleotide Motifs030304 developmental biologyMessenger RNAmetabolism [Nerve Tissue Proteins]RNAmetabolism [Protein Phosphatase 2]General ChemistryProtein phosphatase 2Molecular biologynervous system diseasesProtein Biosynthesisbiology.proteinTrinucleotide repeat expansionTrinucleotide Repeat Expansion030217 neurology & neurosurgeryMid1 protein humanHeLa CellsTranscription FactorsNature communications
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Molecular Basis of SARS-CoV-2 Nsp1-Induced Immune Translational Shutdown as Revealed by All-Atom Simulations.

2021

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic represents the most severe global health crisis in modern human history. One of the major SARS-CoV-2 virulence factors is nonstructural protein 1 (Nsp1), which, outcompeting with the binding of host mRNA to the human ribosome, triggers a translation shutdown of the host immune system. Here, microsecond-long all-atom simulations of the C-terminal portion of the SARS-CoV-2/SARS-CoV Nsp1 in complex with the 40S ribosome disclose that SARS-CoV-2 Nsp1 has evolved from its SARS-CoV ortholog to more effectively hijack the ribosome by undergoing a critical switch of Q/E158 and E/Q159 residues that perfects Nsp1's interactions…

virusesSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)VirulenceBiologyMolecular Dynamics SimulationViral Nonstructural ProteinsRibosomeImmune systemHumansGeneral Materials ScienceEukaryotic Small Ribosomal SubunitPhysical and Theoretical Chemistryskin and connective tissue diseasesRibosome Subunits Small EukaryoticMessenger RNANSP1SARS-CoV-2fungivirus diseasesCOVID-19Translation (biology)Hydrogen BondingCell biologybody regionsSettore CHIM/03 - Chimica Generale E InorganicaProtein BindingThe journal of physical chemistry letters
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