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Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 1986. 46: 705-716.
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2006
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Molecular RegulationGeneticsImmune RegulationImmunologyMolecular BiologyImmunologic MechanismEpigeneticsTranscriptional RegulationImmunogeneticsProtein ExpressionCell RegulationSv40 EnhancerMultiple Nuclear FactorsHeavy ChainOctamer SequenceCell SignalingMolecular SignalingCell 1986Gene ExpressionImmunoglobulin Enhancer SequencesEpigenetic RegulationCell BiologyTranscription RegulationGene FunctionChromatin StructureNatural SciencesGene RegulationImmunoglobulin ETranscription FactorsMedicineCell Development
To characterize proteins that bind to the immunoglobulin (Ig) heavy chain and the κ light chain enhancers, an electrophoretic mobility shift assay with end-labeled DNA fragments was used. Three binding proteins have been found. One is NF-A, a factor found in all tested cell types that binds to the octamer sequence found upstream of all Ig variable region gene segments and to the same octamer In the heavy chain enhancer. The second, also ubiquitous, protein binds to a sequence In both the heavy chain and the K enhancers that was previously shown to be protected from methylation in vivo. Other closely related sites do not compete for this binding, implying a restriction enzyme-like binding specificity. The third protein binds to a sequence In the K enhancer (and to an identical sequence in the SV40 enhancer) and is restricted in Its occurrence to B cells.