Search results for "Nuclear cap-binding protein complex"

showing 3 items of 3 documents

Physical and Genetic Interactions Link the Yeast Protein Zds1p with mRNA Nuclear Export

2005

Eukaryotic gene expression requires the export of mRNA from the nucleus to the cytoplasm. The DEAD box protein Dbp5p is an essential export factor conserved from yeast to man. A fraction of Dbp5p forms a complex with nucleoporins of the cytoplasmic filaments of the nuclear pore complex. Gfd1p was identified originally as a multicopy suppressor of the rat8-2 ts allele of DBP5. Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens. By using the two-hybrid system, we showed that Zds1p interacts in vivo with both Gfd1p and Dbp5p. In vitro binding experiments revealed that Gfd1p and Dbp5p bind directl…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataMutantActive Transport Cell NucleusSaccharomyces cerevisiaeBiologyBiochemistryCytosolGene expressionmedicineRNA MessengerNuclear poreNuclear export signalMolecular BiologyAdaptor Proteins Signal TransducingDNA PrimersGeneticsMessenger RNABase SequenceNuclear cap-binding protein complexRNA FungalCell BiologyCell biologyCell nucleusmedicine.anatomical_structureNucleoporinGenome FungalJournal of Biological Chemistry
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Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
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Purification of a glucose-binding protein from rat liver nuclei. Evidence for a role in targeting of nuclear mRNP to nuclear pore complex.

1992

A nuclear carbohydrate-binding protein with a molecular mass of 67 kDa (CBP67), which is specific for glucose residues, was purified to essential homogeneity from rat liver nuclear extracts. This protein could also be isolated from nuclear ribonucleoprotein (RNP) complexes by extraction in the presence of 0.6 M or 2 M NaCl, but it was absent in polysomal RNP complex. The binding of the purified protein, which has an isoelectric point of 7.3, to glucose-containing glycoconjugates depends on the presence of Ca2+ and Mg2+. Using closed nuclear envelope vesicles as a system to study nuclear transport of RNA, it was shown that both entrapped polysomal mRNA and nuclear RNA precursors are readily …

MaleMonosaccharide Transport ProteinsCations DivalentBiologyBiochemistryAnimalsHumansMagnesiumRNA MessengerNuclear proteinNuclear poreCell NucleusBinding proteinNuclear cap-binding protein complexBiological TransportRats Inbred StrainsRatsMessenger RNPGlucose bindingMolecular WeightBiochemistryLiverRibonucleoproteinsCalciumElectrophoresis Polyacrylamide GelNucleoporinNuclear transportIsoelectric FocusingHeLa CellsEuropean journal of biochemistry
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