Search results for "Histone Chaperones"

showing 3 items of 3 documents

The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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The ribosome assembly gene network is controlled by the feedback regulation of transcription elongation

2017

Ribosome assembly requires the concerted expression of hundreds of genes, which are transcribed by all three nuclear RNA polymerases. Transcription elongation involves dynamic interactions between RNA polymerases and chromatin. We performed a synthetic lethal screening in Saccharomyces cerevisiae with a conditional allele of SPT6, which encodes one of the factors that facilitates this process. Some of these synthetic mutants corresponded to factors that facilitate pre-rRNA processing and ribosome biogenesis. We found that the in vivo depletion of one of these factors, Arb1, activated transcription elongation in the set of genes involved directly in ribosome assembly. Under these depletion c…

0301 basic medicineRibosomal ProteinsSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticCèl·lulesÀcids nucleicsGene regulatory networkRibosome biogenesisSaccharomyces cerevisiaeBiologyRibosome assembly03 medical and health sciencesRegulació genèticaGeneticsGene Regulatory NetworksHistone ChaperonesRNA Processing Post-TranscriptionalGeneAdenosine TriphosphatasesFeedback PhysiologicalMessenger RNAOrganelle BiogenesisGene regulation Chromatin and EpigeneticsRNAChromatinCell biology030104 developmental biologyRNA RibosomalMutationATP-Binding Cassette TransportersOrganelle biogenesisTranscriptional Elongation FactorsSynthetic Lethal MutationsTranscriptomeRibosomes
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Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1

2014

13 páginas, 7 figuras, 2 yablas

Saccharomyces cerevisiae ProteinsTranscription Genetic(5-10) yAsf1Histone H2B ubiquitinationCell Cycle ProteinsSAGASaccharomyces cerevisiaeBiologyyeastMethylationTREX-2RNA TransportHistonesSus1Histone H3Histone H1Gene Expression Regulation FungalhistonesHistone H2ANucleosomeHistone codeTAP-MS strategyHistone ChaperonesRNA MessengerHistone octamerGeneticsNuclear ProteinsRNA-Binding ProteinsAcetylationCell BiologyYeastCell biologyRibonucleoproteinsHistone methyltransferaseProtein Processing Post-TranslationalMolecular ChaperonesResearch Paper
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