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 journalArticlepeer-review

276 Scopus citations


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)
Pages (from-to)1049
Number of pages1
Issue number5
StatePublished - Nov 21 2013
Externally publishedYes

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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