0000000000243140

AUTHOR

Yoshiyuki Kuchino

showing 5 related works from this author

Inhibition of expression of natural UAG suppressor glutamine tRNA in HIV-infected human H9 cells in vitro by Avarol.

1988

HTLV-IIIB-infected H9 cells are shown to contain a high level of the natural UAG suppressor glutamine tRNA(UmUG Gln); this tRNA has been demonstrated to be required for the synthesis of Moloney murine leukemia virus (Mo-MuLV)-encoded protease. After cultivation of HTLV-IIIB-infected H9 cells with Avarol at a concentration (1 microgram/ml), previously found to protect the cells against the cytopathic effects of HTLV-III, an almost complete inhibition of the synthesis of the tRNA(UmUG Gln) was observed. Moreover, we obtained some evidence that the processing of the HTLV-III precursor protein p53 to p24 is inhibited by Avarol in infected cells, suggesting that the compound interferes with the …

ReticulocytesvirusesGlutamineImmunologyBiologyAntiviral AgentsViruslaw.inventionCell LineSuppression GeneticlawVirologyRNA Transfer GlnGene expressionAnimalsHumansCodonvirus diseasesHIVNucleic Acid HybridizationBiological activitybiochemical phenomena metabolism and nutritionRNA Transfer Amino Acid-SpecificCell Transformation ViralMolecular biologyIn vitroGlutamineTobacco Mosaic VirusInfectious DiseasesCell cultureProtein BiosynthesisTransfer RNASuppressorRNA ViralRabbitsSesquiterpenesAIDS research and human retroviruses
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Evidence for involvement of a nuclear envelope-associated RNA helicase activity in nucleocytoplasmic RNA transport

1990

It seems well established that translocation of at least some mRNAs through the nuclear pore is (1) an energy-dependent process, and (2) dependent on the presence of the poly(A) segment attached to most mRNA species. We describe that RNA helicase (RNA duplex unwindase) activity is present in a nuclear envelope (NE) preparation, which also appears to be involved in nucleocytoplasmic RNA transport. This activity unwinds RNA: RNA hybrids. The helicase has a pH optimum of 7.5 and a temperature optimum of 30 degrees C. Applying the sealed NE vesicle system, it was shown that duplex RNA species are readily released from the vesicles in an unidirectional manner, in contrast to single-stranded RNA,…

PhysiologyClinical BiochemistryRNARNA-dependent RNA polymeraseRNA transportCell BiologyBiologyNon-coding RNARNA Helicase ABiochemistryRNA polymerase IBiophysicsDegradosomeSmall nuclear RNAJournal of Cellular Physiology
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Protection of HeLa‐T4 + cells against human immunodeficiency virus (HIV) infection after stable transfection with HIV LTR‐2‘,5‘‐oligoadenylate synthe…

1990

An expression vector (pU3R-III/2-5AS) of human 2',5'-oligoadenylate (2-5A) synthetase was constructed in which a cDNA encoding an active form of the enzyme was located 3' to a 3'-long terminal repeat (LTR) of human immunodeficiency virus type 1 (HIV-1). The LTR-directed expression of this hybrid DNA could be activated in trans by the HIV tat gene product. This vector was used for transfection of HeLa-T4+ cells, which are permissive to HIV infection, as well as of normal HeLa cells. HIV replication after infection of the CD4-receptor-bearing HeLa-T4+ cells with HIV-1 was found to be strongly reduced when drug-selected cells cotransfected with pU3R-III/2-5AS and a hygromycin B resistance gene…

Expression vector2'-5'-OligoadenylatevirusesTransfectionBiologyBiochemistryVirologyMolecular biologyVirusLong terminal repeatGene productchemistry.chemical_compoundchemistryGeneticsMolecular BiologyHygromycin BSelectable markerBiotechnologyThe FASEB Journal
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Inhibitory effect of nonviable preparations from human immunodeficiency virus 1 on inositol phospholipid metabolism

1989

Previously it was established [Pahwa, S., Pahwa, R., Saxinger, C., Gallo, R. C. & Good, R. A. (1985) Proc. Natl Acad. Sci. USA 82, 8198] that nonviable preparations of human immunodeficiency virus 1 (HIV-1) abolish the proliferative response of human lymphocytes to phytohemagglutinin A. Now we describe that this effect might be, at least partially, due to an impairment of the function of phospholipase C. It was found that addition of HIV-1 preparation to lymphocytes diminished the stimulation of phosphatidylinositol phosphorylation caused by phytohemagglutinin A. Moreover, this preparation completely abolished the phytohemagglutinin-A-stimulated release of inositol trisphosphate and prevent…

Inositol PhosphatesInositol 145-TrisphosphateBiologyPhospholipasePhosphatidylinositolsBiochemistrychemistry.chemical_compoundCytosolCyclic AMPPhosphatidylinositol phosphorylationHumansInositolLymphocytesPhosphorylationPhytohemagglutininsInositol phosphateProtein kinase AProtein Kinase CProtein kinase Cchemistry.chemical_classificationCell MembraneVirionBiological TransportInositol trisphosphateMolecular biologyCytosolchemistryBiochemistryType C PhospholipasesHIV-1Sugar PhosphatesCell DivisionEuropean Journal of Biochemistry
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Regulated expression and phosphorylation of the 23-26-kDa ras protein in the sponge Geodia cydonium.

1990

We have cloned, sequenced and examined the sponge Geodia cydonium cDNA encoding a protein homologous to ras proteins. The sponge ras protein has a more conserved N-terminal region and a less conserved C-terminal region, especially in comparison to Dictyostelium discoideum; the similarity to human c-Ha-ras-1 and to Saccharomyces cerevisiae is less pronounced. The sponge ras cDNA comprises five TAG triplets; at the translational level these UAG termination codons are suppressed by a Gln-tRNA. The sponge ras protein was isolated and partially purified (23-26 kDa) and found to undergo phosphorylation at a threonine moiety, when dissociated cells were incubated in the presence of a homologous ag…

GTP'Saccharomyces cerevisiaeMolecular Sequence DataGTPaseBiochemistryDictyostelium discoideumProto-Oncogene Proteins p21(ras)Complementary DNASequence Homology Nucleic AcidAnimalsInsulinNCK1Amino Acid SequenceThreonineCloning MolecularPhosphorylationGene LibrarybiologyBase SequenceDNAbiology.organism_classificationMolecular biologyPoriferaMolecular WeightKineticsBiochemistryGene Expression RegulationPhosphorylationEuropean journal of biochemistry
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