0000000000625730

AUTHOR

Michael Yarus

showing 3 related works from this author

Poly(U) RNA-templated synthesis of AppA.

2015

Simple nucleotide templating activities are of interest as potential primordial reactions. Here we describe the acceleration of 5′-5′ AppA synthesis by 3′-5′ poly(U) under normal solution conditions. This reaction is apparently templated via complementary U:A base-pairing, despite the involvement of two different RNA backbones, because poly(U), unlike other polymers, significantly stimulates AppA synthesis. These interactions occur in moderate (K+) and (Mg2+) and are temperature sensitive, being more efficient at 10°C than at 4°C, but absent at 20°C. The reaction is only slightly pH sensitive, despite potentially relevant substrate pKa’s. Kinetic data explicitly support production of AppA b…

chemistry.chemical_classificationPoly UbiologyMolecular modelStereochemistryRNASubstrate (chemistry)Chemical reactionCofactorArticlechemistryBiochemistrybiology.proteinMoleculeRNANucleotideMolecular BiologyDinucleoside PhosphatesDinucleoside PhosphatesRNA (New York, N.Y.)
researchProduct

Human tRNA(Sec) associates with HeLa membranes, cell lipid liposomes, and synthetic lipid bilayers.

2012

We have shown previously that simple RNA structures bind pure phospholipid liposomes. However, binding of bona fide cellular RNAs under physiological ionic conditions is shown here for the first time. Human tRNASec contains a hydrophobic anticodon-loop modification: N6-isopentenyladenosine (i6A) adjacent to its anticodon. Using a highly specific double-probe hybridization assay, we show mature human tRNASec specifically retained in HeLa intermediate-density membranes. Further, isolated human tRNASec rebinds to liposomes from isolated HeLa membrane lipids, to a much greater extent than an unmodified tRNASec transcript. To better define this affinity, experiments with pure lipids show that li…

Membrane lipidsLipid BilayersMolecular Sequence DataPhospholipidBiologyArticlechemistry.chemical_compoundMembrane MicrodomainsSphingosineHumansLipid bilayerMolecular BiologyLipid raftLiposomeMembranesSphingosineBase SequenceRNARNA Transfer Amino Acid-SpecificKineticsMembranechemistryBiochemistryLiposomesNucleic Acid ConformationHydrophobic and Hydrophilic InteractionsHeLa CellsRNA (New York, N.Y.)
researchProduct

Specific binding of VegT mRNA localization signal to membranes in Xenopus oocytes

2021

Abstract We have studied the interaction of a VegT mRNA localization signal sequence with the membranes of the mitochondrial cloud in Xenopus oocytes, and the binding of the VegT mRNA signal sequence to the lipid raft regions of the vesicles bounded by ordered and disordered phospholipid bilayers. RNA preference for the membranes of the mitochondrial cloud was confirmed using microscopy of a fluorescence resonance energy transfer from RNA molecules to membranes. Our studies show that VegT mRNA has a higher affinity for ordered regions of lipid bilayers. This conclusion is supported by the dissociation constant measurements for RNA-liposome complex and the visualization of the FRET signal be…

Signal peptideXenopusLipid vesiclesMitochondrial cloudProtein Sorting SignalsXenopus ProteinsXenopus laevis03 medical and health sciencesMembrane MicrodomainsRafts0302 clinical medicineFluorescence Resonance Energy TransferAnimalsLipid bilayerMolecular BiologyLipid raftXenopus oocytes030304 developmental biology0303 health sciencesMessenger RNABinding SitesbiologyChemistryVegT mRNARNACell BiologyMembrane RNAbiology.organism_classificationFörster resonance energy transferLiposomesOocytesFRETBiophysicsFemaleT-Box Domain Proteins030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
researchProduct