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.
journal_name
Celljournal_title
Cellauthors
Kwon I,Kato M,Xiang S,Wu L,Theodoropoulos P,Mirzaei H,Han T,Xie S,Corden JL,McKnight SLdoi
10.1016/j.cell.2013.10.033subject
Has Abstractpub_date
2013-11-21 00:00:00pages
1049-1060issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(13)01351-2journal_volume
155pub_type
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