EMSA from quick coupled in vitro transcription/translation system (TNT).
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posted on 2022-08-11, 17:47 authored by Ellen K. Gagliani, Lisa M. Gutzwiller, Yi Kuang, Yoshinobu Odaka, Phillipp Hoffmeister, Stefanie Hauff, Aleksandra Turkiewicz, Emily Harding-Theobald, Patrick J. Dolph, Tilman Borggrefe, Franz Oswald, Brian Gebelein, Rhett A. KovallFull length Flag-Rbpj WT (lane 1 and 2) binds to DNA in contrast to Flag-Rbpj K195E mutant (lane 5 and 6) and Flag-Rbpj E89G mutant (lane 3 and 4), which interact weakly with DNA. Protein-DNA interaction of Flag-Rbpj WT is shown by complex A (single occupancy, lane 1 and 2), complex A’ (double occupancy, lane 1 and 2) and complex B and B’ with the addition of anti-Flag showing supershifting (lane 2). Bottom panel: Western blot to show similar expression levels of WT and variant Rbpj constructs.
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wild type proteinssingle transcription factorretains cofactor bindinggenetic studies supportgene expression viadiv >< pconverts extracellular receptorantagonistic hairless coanalogous residue foundassociated rbpj variantnotch comammalian cotaken togethersequestering eitherrbpj previously describedopposing manneroliver syndromenull allelenotch signalingmissense mutationlimb defectsligand interactionsdrosophila dominant activitydata suggestconserved pathwayallele encodesallele behave
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