Abstract
The study of Oct4 gene regulation in murine embryonic stem cells revealed that distal enhancer (DE) was its key element. DE includes two functional elements, DEa and DEb. Both elements are required for Oct expression in pluripotent cells. The most feasible nominee for binding with the DEb site is Oct4 protein heterodimerized with Sox2. It is still unclear what transcription proteins bind to the DEa site and how cooperation between DEa and DEb sites is exerted. Using biotinylated oligonucleotides, we developed a sensitive EMSA for DNA-protein complexes. This method, as well as protein chromatographic fractionation, was used to isolate proteins specifically bound with the DEa site of Oct4 DE in extracts of murine embryonic stem cells and tissues.
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