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Cell. 2013 Nov 21;155(5):1049-1060. doi: 10.1016/j.cell.2013.10.033.

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

Author information

1
Department of Biochemistry University of Texas Southwestern Medical Center 5323 Harry Hines Boulevard Dallas, TX 75390-9152.
2
Department of Molecular Biology and Genetics The Johns Hopkins University School of Medicine Baltimore, MD 21205.
#
Contributed equally

Erratum in

  • Cell. 2014 Jan 16;156(1-2):374.

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.

PMID:
24267890
PMCID:
PMC4010232
DOI:
10.1016/j.cell.2013.10.033
[Indexed for MEDLINE]
Free PMC Article

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