The human p52 protein is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II. The function of p52 is through interactions with transcriptional activators and the basal transcription machinery. In addition, p52 may also interact with several cellular proteins including the transcription coactivator PC4, the essential splicing factor ASF/SF2 and the nuclear protein nucleolin.
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Protein-protein interactions have been widely used to study gene expression pathways and may be considered as a new approach to drug discovery. Here I report the development of a universal protein array (UPA) system that provides a sensitive, quantitative, multi-purpose
Increasing evidence suggests that pre-mRNA splicing can take place cotranscriptionally in vivo. However, insight into how these two processes are linked has been lacking. Here, we describe that a novel transcriptional coactivator, p52, interacts not only with transcriptional activators and
Transcriptional activation in human cell-free systems containing RNA polymerase II and general initiation factors requires the action of one or more additional coactivators. Here, we report the isolation of cDNAs encoding two novel human transcriptional coactivators (p52 and p75) that
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