XPhosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains

Ilmin Kwon, Masato Kato, Siheng Xiang, Leeju Wu, Pano Theodoropoulos, Hamid Mirzaei, Tina Han, Shanhai Xie, Jeffry L. Corden, Steven L. McKnight

Research output: Contribution to journalArticle

Abstract

The low-complexity (LC) domains of the products of the fused in sarcoma (FUS), Ewings sarcoma (EWS), and TAF15 genes are translocated onto a variety of different DNA-binding domains and thereby assist in driving the formation of cancerous cells. In the context of the translocated fusion proteins, these LC sequences function as transcriptional activation domains. Here, we show that polymeric fibers formed from these LC domains directly bind the C-terminal domain (CTD) of RNA polymerase II in a manner reversible by phosphorylation of the iterated, heptad repeats of the CTD. Mutational analysis indicates that the degree of binding between the CTD and the LC domain polymers correlates with the strength of transcriptional activation. These studies offer a simple means of conceptualizing how RNA polymerase II is recruited to active genes in its unphosphorylated state and released for elongation following phosphorylation of the CTD. PaperFlick

Original languageEnglish (US)
Number of pages1
JournalCell
Volume155
Issue number5
DOIs
StatePublished - Nov 21 2013

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Kwon, I., Kato, M., Xiang, S., Wu, L., Theodoropoulos, P., Mirzaei, H., Han, T., Xie, S., Corden, J. L., & McKnight, S. L. (2013). XPhosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains. Cell, 155(5). https://doi.org/10.1016/j.cell.2013.10.033