[HTML][HTML] DNA binding by the ETS protein TEL (ETV6) is regulated by autoinhibition and self-association
SM Green, HJ Coyne, LP McIntosh… - Journal of biological …, 2010 - ASBMB
The ETS protein TEL, a transcriptional repressor, contains a PNT domain that, as an isolated
fragment in vitro, self-associates to form a head-to-tail polymer. How such polymerization
might affect the DNA-binding properties of full-length TEL is unclear. Here we report that
monomeric TEL binds to a consensus ETS site with unusually low affinity (K d= 2.8× 10− 8
m). A deletion analysis demonstrated that the low affinity was caused by a C-terminal
inhibitory domain (CID) that attenuates DNA binding by∼ 10-fold. An NMR spectroscopically …
fragment in vitro, self-associates to form a head-to-tail polymer. How such polymerization
might affect the DNA-binding properties of full-length TEL is unclear. Here we report that
monomeric TEL binds to a consensus ETS site with unusually low affinity (K d= 2.8× 10− 8
m). A deletion analysis demonstrated that the low affinity was caused by a C-terminal
inhibitory domain (CID) that attenuates DNA binding by∼ 10-fold. An NMR spectroscopically …
