Abstract
Ternary complex factors (TCFs), a subgroup of the ets protein family, bind with a dimer of serum response factor to the c-fos serum response element. Both DNA binding and transcriptional activation by TCFs are regulated by mitogen-activated protein kinases. When activated, mitogen-activated protein kinases form homodimers that translocate to the nucleus, where they interact with TCFs via specific docking sites. Here we show by three different criteria that Elk-1 is capable of forming dimers in eukaryotic cells through two distinct interaction domains. These observations are consistent with a dynamic model of TCF-promoter interactions.
Highlights
Ternary complex factors (TCFs)1 were first identified through their interactions with serum response factor (SRF) at the c-fos serum response element (SRE) [1]
Given that interactions between promoters and TCFs are dynamic and, in the absence of any data suggesting that TCFs and extracellular signal-regulated kinases (ERKs) can form stable, DNA-bound complexes, we hypothesized that TCFs may have the capacity to form dimers
This result may be due to the formation of complexes between Elk-1 and other proteins, this is unlikely given the different sources of Elk-1 and the fact that it was overexpressed in both systems
Summary
Ternary complex factors (TCFs)1 were first identified through their interactions with serum response factor (SRF) at the c-fos serum response element (SRE) [1]. To rule out the possibility that the high apparent molecular mass of Elk-1 expressed in COS cells was due to interactions with either SRF or MAPKs, Elk-1 proteins lacking each of these short domains (see Fig. 4A) were overexpressed, and their oligomeric status was assessed.
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